| Year |
Citation |
Score |
| 2024 |
Rush KW, Eastman KAS, Welch EF, Bandarian V, Blackburn NJ. Capturing the Binuclear Copper State of Peptidylglycine Monooxygenase Using a Peptidyl-Homocysteine Lure. Journal of the American Chemical Society. PMID 38363651 DOI: 10.1021/jacs.3c14705 |
0.45 |
|
| 2024 |
Roger M, Leone P, Blackburn NJ, Horrell S, Chicano TM, Biaso F, Giudici-Orticoni MT, Abriata LA, Hura GL, Hough MA, Sciara G, Ilbert M. Beyond the coupled distortion model: structural analysis of the single domain cupredoxin AcoP, a green mononuclear copper centre with original features. Dalton Transactions (Cambridge, England : 2003). PMID 38170898 DOI: 10.1039/d3dt03372d |
0.497 |
|
| 2023 |
Arias RJ, Welch EF, Blackburn NJ. New structures reveal flexible dynamics between the subdomains of peptidylglycine monooxygenase. Implications for an open to closed mechanism. Protein Science : a Publication of the Protein Society. 32: e4615. PMID 36880254 DOI: 10.1002/pro.4615 |
0.492 |
|
| 2022 |
Welch EF, Rush KW, Arias RJ, Blackburn NJ. Pre-Steady-State Reactivity of Peptidylglycine Monooxygenase Implicates Ascorbate in Substrate Triggering of the Active Conformer. Biochemistry. 61: 665-677. PMID 35380039 DOI: 10.1021/acs.biochem.2c00080 |
0.45 |
|
| 2022 |
Welch EF, Rush KW, Arias RJ, Blackburn NJ. Copper monooxygenase reactivity: Do consensus mechanisms accurately reflect experimental observations? Journal of Inorganic Biochemistry. 231: 111780. PMID 35303611 DOI: 10.1016/j.jinorgbio.2022.111780 |
0.443 |
|
| 2021 |
Grasso M, Bond GJ, Kim YJ, Boyd S, Matson Dzebo M, Valenzuela S, Tsang T, Schibrowsky NA, Alwan KB, Blackburn NJ, Burslem GM, Wittung-Stafshede P, Winkler DD, Marmorstein R, Brady DC. The copper chaperone CCS facilitates copper binding to MEK1/2 to promote kinase activation. The Journal of Biological Chemistry. 101314. PMID 34715128 DOI: 10.1016/j.jbc.2021.101314 |
0.455 |
|
| 2019 |
Morgada MN, Emiliani F, Chacón KN, Álvarez-Paggi D, Murgida DH, Blackburn NJ, Abriata LA, Vila AJ. pH-Induced Binding of the Axial Ligand in an Engineered Cu Site Favors the π State. Inorganic Chemistry. PMID 31710470 DOI: 10.1021/Acs.Inorgchem.9B01868 |
0.542 |
|
| 2019 |
Alwan KB, Welch EF, Blackburn NJ. The Catalytic M-center of Copper Monooxygenases probed by Rational Design. Effects of Selenomethionine and Histidine Substitution on Structure and Reactivity. Biochemistry. PMID 31626532 DOI: 10.1021/Acs.Biochem.9B00823 |
0.641 |
|
| 2019 |
Rao G, Pattenaude SA, Alwan K, Blackburn NJ, Britt RD, Rauchfuss TB. The binuclear cluster of [FeFe] hydrogenase is formed with sulfur donated by cysteine of an [Fe(Cys)(CO)(CN)] organometallic precursor. Proceedings of the National Academy of Sciences of the United States of America. PMID 31570604 DOI: 10.1073/Pnas.1913324116 |
0.327 |
|
| 2019 |
Alwan KB, Welch EF, Arias RJ, Gambill BF, Blackburn NJ. Rational Design of a Histidine-Methionine Site Modeling the M-Center of Copper Monooxygenases in a Small Metallochaperone Scaffold. Biochemistry. PMID 31243953 DOI: 10.1021/Acs.Biochem.9B00312 |
0.56 |
|
| 2018 |
Chacón KN, Perkins J, Mathe Z, Alwan K, Ho EN, Ucisik MN, Merz KM, Blackburn NJ. Trapping intermediates in metal transfer reactions of the CusCBAF export pump of . Communications Biology. 1: 192. PMID 30456313 DOI: 10.1038/s42003-018-0181-9 |
0.387 |
|
| 2018 |
Maheshwari S, Shimokawa C, Rudzka K, Kline CD, Eipper BA, Mains RE, Gabelli SB, Blackburn N, Amzel LM. Effects of copper occupancy on the conformational landscape of peptidylglycine α-hydroxylating monooxygenase. Communications Biology. 1: 74. PMID 30271955 DOI: 10.1038/s42003-018-0082-y |
0.364 |
|
| 2017 |
Fetherolf MM, Boyd SD, Taylor AB, Kim HJ, Wohlschlegel JA, Blackburn NJ, Hart PJ, Winge DR, Winkler DD. Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper-ion entry site. The Journal of Biological Chemistry. PMID 28533431 DOI: 10.1074/Jbc.M117.775981 |
0.53 |
|
| 2016 |
Kline CD, Blackburn NJ. Substrate-Induced Carbon Monoxide Reactivity Suggests Multiple Enzyme Conformations at the Catalytic Copper M-Center of Peptidylglycine Monooxygenase. Biochemistry. 55: 6652-6661. PMID 27933800 DOI: 10.1021/Acs.Biochem.6B00845 |
0.481 |
|
| 2016 |
Yu Y, Petrik I, Chacón KN, Hosseinzadeh P, Chen H, Blackburn NJ, Lu Y. Effect of Circular Permutation on the Structure and Function of Type 1 Blue Copper Center in Azurin. Protein Science : a Publication of the Protein Society. PMID 27759897 DOI: 10.1002/Pro.3071 |
0.403 |
|
| 2016 |
Tian S, Liu J, Cowley RE, Hosseinzadeh P, Marshall NM, Yu Y, Robinson H, Nilges MJ, Blackburn NJ, Solomon EI, Lu Y. Reversible S-nitrosylation in an engineered azurin. Nature Chemistry. 8: 670-7. PMID 27325093 DOI: 10.1038/Nchem.2489 |
0.512 |
|
| 2016 |
Kline CD, Gambill BF, Mayfield M, Lutsenko S, Blackburn NJ. pH-regulated metal-ligand switching in the HM loop of ATP7A: a new paradigm for metal transfer chemistry. Metallomics : Integrated Biometal Science. PMID 27242196 DOI: 10.1039/C6Mt00062B |
0.406 |
|
| 2016 |
Chauhan S, Hosseinzadeh P, Lu Y, Blackburn NJ. Stopped-Flow Studies of the Reduction of the Copper Centers Suggest a Bifurcated Electron Transfer Pathway in Peptidylglycine Monooxygenase. Biochemistry. PMID 26982589 DOI: 10.1021/Acs.Biochem.6B00061 |
0.379 |
|
| 2016 |
Martin-Diaconescu V, Chacón KN, Delgado-Jaime MU, Sokaras D, Weng TC, DeBeer S, Blackburn NJ. Kβ Valence to Core X-ray Emission Studies of Cu(I) Binding Proteins with Mixed Methionine - Histidine Coordination. Relevance to the Reactivity of the M- and H-sites of Peptidylglycine Monooxygenase. Inorganic Chemistry. PMID 26965786 DOI: 10.1021/Acs.Inorgchem.5B02842 |
0.634 |
|
| 2015 |
Chakraborty S, Polen MA, Chacón KN, Wilson TD, Yu Y, Reed J, Nilges MJ, Blackburn NJ, Lu Y. Binuclear CuA Formation in Biosynthetic Models of CuA in Azurin Proceeds via a Novel Cu(Cys)2His Mononuclear Copper Intermediate. Biochemistry. PMID 26352296 DOI: 10.1021/Acs.Biochem.5B00659 |
0.602 |
|
| 2015 |
Butterfield CN, Tao L, Chacón KN, Spiro TG, Blackburn NJ, Casey WH, Britt RD, Tebo BM. Multicopper manganese oxidase accessory proteins bind Cu and heme. Biochimica Et Biophysica Acta. 1854: 1853-9. PMID 26327317 DOI: 10.1016/J.Bbapap.2015.08.012 |
0.602 |
|
| 2014 |
Chacón KN, Mealman TD, McEvoy MM, Blackburn NJ. Tracking metal ions through a Cu/Ag efflux pump assigns the functional roles of the periplasmic proteins. Proceedings of the National Academy of Sciences of the United States of America. 111: 15373-8. PMID 25313055 DOI: 10.1073/Pnas.1411475111 |
0.503 |
|
| 2014 |
Park GY, Lee JY, Himes RA, Thomas GS, Blackburn NJ, Karlin KD. Copper-peptide complex structure and reactivity when found in conserved His-X(aa)-His sequences. Journal of the American Chemical Society. 136: 12532-5. PMID 25171435 DOI: 10.1021/Ja505098V |
0.622 |
|
| 2014 |
Clark KM, Yu Y, van der Donk WA, Blackburn N, Lu Y. Modulating the Copper-Sulfur Interaction in Type 1 Blue Copper Azurin by Replacing Cys112 with Nonproteinogenic Homocysteine. Inorganic Chemistry Frontiers. 1: 153-158. PMID 24707355 DOI: 10.1039/C3Qi00096F |
0.593 |
|
| 2014 |
Chauhan S, Kline CD, Mayfield M, Blackburn NJ. Binding of copper and silver to single-site variants of peptidylglycine monooxygenase reveals the structure and chemistry of the individual metal centers Biochemistry. 53: 1069-1080. PMID 24471980 DOI: 10.1021/Bi4015264 |
0.64 |
|
| 2014 |
Blackburn NJ, Yan N, Lutsenko S. Copper in eukaryotes Rsc Metallobiology. 2014: 524-555. |
0.432 |
|
| 2013 |
Kline CD, Mayfield M, Blackburn NJ. HHM motif at the CuH-Site of peptidylglycine monooxygenase is a pH-dependent conformational switch Biochemistry. 52: 2586-2596. PMID 23530865 DOI: 10.1021/Bi4002248 |
0.522 |
|
| 2013 |
Osborne RL, Zhu H, Iavarone AT, Blackburn NJ, Klinman JP. Interdomain long-range electron transfer becomes rate-limiting in the Y216A variant of tyramine β-monooxygenase Biochemistry. 52: 1179-1191. PMID 23320946 DOI: 10.1021/Bi3013609 |
0.556 |
|
| 2012 |
Abriata LA, Álvarez-Paggi D, Ledesma GN, Blackburn NJ, Vila AJ, Murgida DH. Alternative ground states enable pathway switching in biological electron transfer. Proceedings of the National Academy of Sciences of the United States of America. 109: 17348-53. PMID 23054836 DOI: 10.1073/Pnas.1204251109 |
0.329 |
|
| 2012 |
Mealman TD, Blackburn NJ, McEvoy MM. Metal export by CusCFBA, the periplasmic Cu(I)/Ag(I) transport system of Escherichia coli. Current Topics in Membranes. 69: 163-96. PMID 23046651 DOI: 10.1016/B978-0-12-394390-3.00007-0 |
0.476 |
|
| 2012 |
Chacón KN, Blackburn NJ. Stable Cu(II) and Cu(I) mononuclear intermediates in the assembly of the CuA center of Thermus thermophilus cytochrome oxidase. Journal of the American Chemical Society. 134: 16401-12. PMID 22946616 DOI: 10.1021/Ja307276Z |
0.591 |
|
| 2012 |
Mealman TD, Zhou M, Affandi T, Chacón KN, Aranguren ME, Blackburn NJ, Wysocki VH, McEvoy MM. N-terminal region of CusB is sufficient for metal binding and metal transfer with the metallochaperone CusF. Biochemistry. 51: 6767-75. PMID 22812620 DOI: 10.1021/Bi300596A |
0.401 |
|
| 2012 |
Otoikhian A, Barry AN, Mayfield M, Nilges M, Huang Y, Lutsenko S, Blackburn NJ. Lumenal loop M672-P707 of the menkes protein (ATP7A) transfers copper to peptidylglycine monooxygenase Journal of the American Chemical Society. 134: 10458-10468. PMID 22577880 DOI: 10.1021/Ja301221S |
0.615 |
|
| 2011 |
Bauman AT, Broers BA, Kline CD, Blackburn NJ. A copper-methionine interaction controls the pH-dependent activation of peptidylglycine monooxygenase. Biochemistry. 50: 10819-28. PMID 22080626 DOI: 10.1021/Bi201193J |
0.524 |
|
| 2011 |
Barry AN, Otoikhian A, Bhatt S, Shinde U, Tsivkovskii R, Blackburn NJ, Lutsenko S. The lumenal loop Met672-Pro707 of copper-transporting ATPase ATP7A binds metals and facilitates copper release from the intramembrane sites. The Journal of Biological Chemistry. 286: 26585-94. PMID 21646353 DOI: 10.1074/Jbc.M111.229039 |
0.584 |
|
| 2011 |
Siluvai GS, Nakano M, Mayfield M, Blackburn NJ. The essential role of the Cu(II) state of Sco in the maturation of the CuA center of cytochrome oxidase: Evidence from H135Met and H135SeM variants of the Bacillus subtilis Sco Journal of Biological Inorganic Chemistry. 16: 285-297. PMID 21069401 DOI: 10.1007/S00775-010-0725-Z |
0.593 |
|
| 2010 |
Clark KM, Yu Y, Marshall NM, Sieracki NA, Nilges MJ, Blackburn NJ, van der Donk WA, Lu Y. Transforming a blue copper into a red copper protein: engineering cysteine and homocysteine into the axial position of azurin using site-directed mutagenesis and expressed protein ligation. Journal of the American Chemical Society. 132: 10093-101. PMID 20608676 DOI: 10.1021/Ja102632P |
0.575 |
|
| 2010 |
Hess CR, Klinman JP, Blackburn NJ. The copper centers of tyramine β-monooxygenase and its catalytic-site methionine variants: An X-ray absorption study Journal of Biological Inorganic Chemistry. 15: 1195-1207. PMID 20544364 DOI: 10.1007/S00775-010-0677-3 |
0.614 |
|
| 2010 |
Siluvai GS, Mayfield M, Nilges MJ, Debeer George S, Blackburn NJ. Anatomy of a red copper center: Spectroscopic identification and reactivity of the copper centers of bacillus subtilis Sco and its Cys-to-ala variants Journal of the American Chemical Society. 132: 5215-5226. PMID 20232870 DOI: 10.1021/Ja910759V |
0.609 |
|
| 2010 |
Blackburn NJ. A tale of two metals. Chemistry & Biology. 17: 8-9. PMID 20142035 DOI: 10.1016/J.Chembiol.2010.01.004 |
0.416 |
|
| 2010 |
LeShane ES, Shinde U, Walker JM, Barry AN, Blackburn NJ, Ralle M, Lutsenko S. Interactions between copper-binding sites determine the redox status and conformation of the regulatory N-terminal domain of ATP7B. The Journal of Biological Chemistry. 285: 6327-36. PMID 20032459 DOI: 10.1074/Jbc.M109.074633 |
0.479 |
|
| 2009 |
Siluvai GS, Nakano MM, Mayfield M, Nilges MJ, Blackburn NJ. H135A controls the redox activity of the Sco copper center. Kinetic and spectroscopic studies of the His135Ala variant of Bacillus subtilis Sco Biochemistry. 48: 12133-12144. PMID 19921776 DOI: 10.1021/Bi901480G |
0.592 |
|
| 2009 |
Loftin IR, Blackburn NJ, McEvoy MM. Tryptophan Cu(I)-pi interaction fine-tunes the metal binding properties of the bacterial metallochaperone CusF. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 14: 905-12. PMID 19381697 DOI: 10.1007/S00775-009-0503-Y |
0.6 |
|
| 2009 |
De Feo CJ, Aller SG, Siluvai GS, Blackburn NJ, Unger VM. Three-dimensional structure of the human copper transporter hCTR1. Proceedings of the National Academy of Sciences of the United States of America. 106: 4237-42. PMID 19240214 DOI: 10.1073/Pnas.0810286106 |
0.569 |
|
| 2009 |
Feo CJD, Aller SG, Barkan Y, Shcushan M, Siluvai G, Ben-Tal N, Blackburn NJ, Unger VM. CTR Structure and Mechanism Biophysical Journal. 96. DOI: 10.1016/J.Bpj.2008.12.004 |
0.602 |
|
| 2008 |
Barry AN, Clark KM, Otoikhian A, van der Donk WA, Blackburn NJ. Selenocysteine positional variants reveal contributions to copper binding from cysteine residues in domains 2 and 3 of human copper chaperone for superoxide dismutase. Biochemistry. 47: 13074-83. PMID 19007184 DOI: 10.1021/Bi801438G |
0.507 |
|
| 2008 |
Himes RA, Park GY, Siluvai GS, Blackburn NJ, Karlin KD. Structural studies of copper(I) complexes of amyloid-beta peptide fragments: formation of two-coordinate bis(histidine) complexes. Angewandte Chemie (International Ed. in English). 47: 9084-7. PMID 18932185 DOI: 10.1002/Anie.200803908 |
0.443 |
|
| 2008 |
Bagai I, Rensing C, Blackburn NJ, McEvoy MM. Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone. Biochemistry. 47: 11408-14. PMID 18847219 DOI: 10.1021/Bi801638M |
0.425 |
|
| 2008 |
Barry AN, Blackburn NJ. A selenocysteine variant of the human copper chaperone for superoxide dismutase. A Se-XAS probe of cluster composition at the domain 3-domain 3 dimer interface. Biochemistry. 47: 4916-28. PMID 18393442 DOI: 10.1021/Bi8001049 |
0.48 |
|
| 2007 |
Stasser JP, Siluvai GS, Barry AN, Blackburn NJ. A multinuclear copper(I) cluster forms the dimerization interface in copper-loaded human copper chaperone for superoxide dismutase. Biochemistry. 46: 11845-56. PMID 17902702 DOI: 10.1021/Bi700566H |
0.464 |
|
| 2007 |
Loftin IR, Franke S, Blackburn NJ, McEvoy MM. Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy. Protein Science : a Publication of the Protein Society. 16: 2287-93. PMID 17893365 DOI: 10.1110/Ps.073021307 |
0.567 |
|
| 2007 |
Bagai I, Liu W, Rensing C, Blackburn NJ, McEvoy MM. Substrate-linked conformational change in the periplasmic component of a Cu(I)/Ag(I) efflux system. The Journal of Biological Chemistry. 282: 35695-702. PMID 17893146 DOI: 10.1074/Jbc.M703937200 |
0.538 |
|
| 2007 |
Himes RA, Park GY, Barry AN, Blackburn NJ, Karlin KD. Synthesis and X-ray absorption spectroscopy structural studies of Cu(I) complexes of histidylhistidine peptides: the predominance of linear 2-coordinate geometry. Journal of the American Chemical Society. 129: 5352-3. PMID 17411054 DOI: 10.1021/Ja0708013 |
0.596 |
|
| 2007 |
Ralle M, Blackburn NJ, Lutsenko S. Using XAS and SXRF to study copper in wilson disease at the molecular and tissue level Aip Conference Proceedings. 882: 328-330. DOI: 10.1063/1.2644515 |
0.517 |
|
| 2006 |
Evans JP, Blackburn NJ, Klinman JP. The catalytic role of the copper ligand H172 of peptidylglycine α-hydroxylating monooxygenase: A kinetic study of the H172A mutant Biochemistry. 45: 15419-15429. PMID 17176064 DOI: 10.1021/bi061734c |
0.373 |
|
| 2006 |
Bauman AT, Jaron S, Yukl ET, Burchfiel JR, Blackburn NJ. pH Dependence of peptidylglycine monooxygenase. Mechanistic implications of Cu-methionine binding dynamics. Biochemistry. 45: 11140-50. PMID 16964975 DOI: 10.1021/Bi060905A |
0.385 |
|
| 2006 |
De M, Bell J, Blackburn NJ, Mains RE, Eipper BA. Role for an essential tyrosine in peptide amidation. The Journal of Biological Chemistry. 281: 20873-82. PMID 16704972 DOI: 10.1074/Jbc.M513886200 |
0.358 |
|
| 2006 |
Bauman AT, Yukl ET, Alkevich K, McCormack AL, Blackburn NJ. The hydrogen peroxide reactivity of peptidylglycine monooxygenase supports a Cu(II)-superoxo catalytic intermediate. The Journal of Biological Chemistry. 281: 4190-8. PMID 16330540 DOI: 10.1074/Jbc.M511199200 |
0.404 |
|
| 2005 |
Andruzzi L, Nakano M, Nilges MJ, Blackburn NJ. Spectroscopic studies of metal binding and metal selectivity in Bacillus subtilis BSco, a Homologue of the Yeast Mitochondrial Protein Sco1p. Journal of the American Chemical Society. 127: 16548-58. PMID 16305244 DOI: 10.1021/Ja0529539 |
0.588 |
|
| 2005 |
Bandeiras TM, Pereira MM, Teixeira M, Moenne-Loccoz P, Blackburn NJ. Structure and coordination of CuB in the Acidianus ambivalens aa3 quinol oxidase heme-copper center. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 10: 625-35. PMID 16163550 DOI: 10.1007/S00775-005-0012-6 |
0.623 |
|
| 2005 |
Siebert X, Eipper BA, Mains RE, Prigge ST, Blackburn NJ, Amzel LM. The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural role. Biophysical Journal. 89: 3312-9. PMID 16100265 DOI: 10.1529/Biophysj.105.066100 |
0.39 |
|
| 2005 |
Stasser JP, Eisses JF, Barry AN, Kaplan JH, Blackburn NJ. Cysteine-to-serine mutants of the human copper chaperone for superoxide dismutase reveal a copper cluster at a domain III dimer interface. Biochemistry. 44: 3143-52. PMID 15736924 DOI: 10.1021/Bi0478392 |
0.573 |
|
| 2005 |
Ghiladi RA, Huang HW, Moënne-Loccoz P, Stasser J, Blackburn NJ, Woods AS, Cotter RJ, Incarvito CD, Rheingold AL, Karlin KD. Heme-copper/dioxygen adduct formation relevant to cytochrome c oxidase: spectroscopic characterization of [(6L)FeIII-(O2(2-))-CuII]+. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 10: 63-77. PMID 15583964 DOI: 10.1007/S00775-004-0609-1 |
0.448 |
|
| 2004 |
Ralle M, Berry SM, Nilges MJ, Gieselman MD, van der Donk WA, Lu Y, Blackburn NJ. The selenocysteine-substituted blue copper center: spectroscopic investigations of Cys112SeCys Pseudomonas aeruginosa azurin. Journal of the American Chemical Society. 126: 7244-56. PMID 15186162 DOI: 10.1021/Ja031821H |
0.576 |
|
| 2004 |
Ralle M, Lutsenko S, Blackburn NJ. Copper transfer to the N-terminal domain of the Wilson disease protein (ATP7B): X-ray absorption spectroscopy of reconstituted and chaperone-loaded metal binding domains and their interaction with exogenous ligands. Journal of Inorganic Biochemistry. 98: 765-74. PMID 15134922 DOI: 10.1016/J.Jinorgbio.2004.02.009 |
0.535 |
|
| 2004 |
Walker JM, Huster D, Ralle M, Morgan CT, Blackburn NJ, Lutsenko S. The N-terminal metal-binding site 2 of the Wilson's Disease Protein plays a key role in the transfer of copper from Atox1. The Journal of Biological Chemistry. 279: 15376-84. PMID 14754885 DOI: 10.1074/Jbc.M400053200 |
0.562 |
|
| 2003 |
Okeley NM, Paul M, Stasser JP, Blackburn N, van der Donk WA. SpaC and NisC, the cyclases involved in subtilin and nisin biosynthesis, are zinc proteins. Biochemistry. 42: 13613-24. PMID 14622008 DOI: 10.1021/Bi0354942 |
0.418 |
|
| 2003 |
Berry SM, Ralle M, Low DW, Blackburn NJ, Lu Y. Probing the role of axial methionine in the blue copper center of azurin with unnatural amino acids. Journal of the American Chemical Society. 125: 8760-8. PMID 12862470 DOI: 10.1021/Ja029699U |
0.522 |
|
| 2003 |
Ralle M, Lutsenko S, Blackburn NJ. X-ray absorption spectroscopy of the copper chaperone HAH1 reveals a linear two-coordinate Cu(I) center capable of adduct formation with exogenous thiols and phosphines. The Journal of Biological Chemistry. 278: 23163-70. PMID 12686548 DOI: 10.1074/Jbc.M303474200 |
0.655 |
|
| 2003 |
Francisco WA, Blackburn NJ, Klinman JP. Oxygen and hydrogen isotope effects in an active site tyrosine to phenylalanine mutant of peptidylglycine alpha-hydroxylating monooxygenase: mechanistic implications. Biochemistry. 42: 1813-9. PMID 12590568 DOI: 10.1021/Bi020592T |
0.406 |
|
| 2003 |
Lu Y, Berry SM, Gieselman MD, Ralle M, Low DW, van der Donk WA, Blackburn NJ. Introducing unnatural amino acids into protein metal-binding sites and its role in metalloprotein design and engineering Journal of Inorganic Biochemistry. 96: 181. DOI: 10.1016/S0162-0134(03)80694-3 |
0.323 |
|
| 2003 |
Blackburn NJ, Ralle M, Lutsenko S, Kaplan J, Eisses J, Stasser J. X-ray absorption studies of copper chaperones Journal of Inorganic Biochemistry. 96: 43. DOI: 10.1016/S0162-0134(03)80477-4 |
0.402 |
|
| 2002 |
Jaron S, Mains RE, Eipper BA, Blackburn NJ. The catalytic role of the copper ligand H172 of peptidylglycine alpha-hydroxylating monooxygenase (PHM): a spectroscopic study of the H172A mutant. Biochemistry. 41: 13274-82. PMID 12403629 DOI: 10.1021/Bi020404Z |
0.593 |
|
| 2001 |
Rhames FC, Murthy NN, Karlin KD, Blackburn NJ. Isocyanide binding to the copper(I) centers of the catalytic core of peptidylglycine monooxygenase (PHMcc). Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 6: 567-77. PMID 11472020 DOI: 10.1007/S007750100233 |
0.699 |
|
| 2001 |
Jaron S, Blackburn NJ. Characterization of a half-apo derivative of peptidylglycine monooxygenase. Insight into the reactivity of each active site copper Biochemistry. 40: 6867-6875. PMID 11389601 DOI: 10.1021/Bi002849Y |
0.585 |
|
| 2000 |
Blackburn NJ, Rhames FC, Ralle M, Jaron S. Major changes in copper coordination accompany reduction of peptidylglycine monooxygenase: implications for electron transfer and the catalytic mechanism. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 5: 341-53. PMID 10907745 DOI: 10.1007/Pl00010663 |
0.7 |
|
| 2000 |
Eisses JF, Stasser JP, Ralle M, Kaplan JH, Blackburn NJ. Domains I and III of the human copper chaperone for superoxide dismutase interact via a cysteine-bridged dicopper(I) cluster Biochemistry. 39: 7337-7342. PMID 10858280 DOI: 10.1021/Bi000690J |
0.615 |
|
| 2000 |
Blackburn NJ, Ralle M, Hassett R, Kosman DJ. Spectroscopic analysis of the trinuclear cluster in the Fet3 protein from yeast, a multinuclear copper oxidase Biochemistry. 39: 2316-2324. PMID 10694398 DOI: 10.1021/Bi992334A |
0.557 |
|
| 1999 |
Jaron S, Blackburn NJ. Does superoxide channel between the copper centers in peptidylglycine monooxygenase? A new mechanism based on carbon monoxide reactivity Biochemistry. 38: 15086-15096. PMID 10563791 DOI: 10.1021/Bi991341W |
0.614 |
|
| 1999 |
Williams PA, Blackburn NJ, Sanders D, Bellamy H, Stura EA, Fee JA, McRee DE. The Cu(A) domain of Thermus thermophilus ba3-type cytochrome C oxidase at 1.6 Å resolution Nature Structural Biology. 6: 509-516. PMID 10360350 DOI: 10.1038/9274 |
0.551 |
|
| 1999 |
Ralle M, Verkhovskaya ML, Morgan JE, Verkhovsky MI, Wikström M, Blackburn NJ. Coordination of CuB in reduced and CO-liganded states of cytochrome bo3 from Escherichia coli. Is chloride ion a cofactor? Biochemistry. 38: 7185-94. PMID 10353829 DOI: 10.1021/Bi982885L |
0.568 |
|
| 1999 |
Blackburn NJ, Ralle M, Gomez E, Hill MG, Pastuszyn A, Sanders D, Fee JA. Selenomethionine-substituted Thermus thermophilus cytochrome ba3: Characterization of the Cu(A) site by Se and Cu K-EXAFS Biochemistry. 38: 7075-7084. PMID 10353818 DOI: 10.1021/Bi982500Z |
0.556 |
|
| 1998 |
Francisco WA, Merkler DJ, Blackburn NJ, Klinman JP. Kinetic mechanism and intrinsic isotope effects for the peptidylglycine alpha-amidating enzyme reaction. Biochemistry. 37: 8244-52. PMID 9609721 DOI: 10.1021/Bi973004Y |
0.321 |
|
| 1998 |
Périé FH, Reddy GVB, Blackburn NJ, Gold MH. Purification and characterization of laccases from the white-rot basidiomycete Dichomitus squalens Archives of Biochemistry and Biophysics. 353: 349-355. PMID 9606969 DOI: 10.1006/Abbi.1998.0625 |
0.406 |
|
| 1998 |
Ralle M, Cooper MJ, Lutsenko S, Blackburn NJ. The menkes disease protein binds copper via novel 2-coordinate Cu(I)- cysteinates in the N-terminal domain [7] Journal of the American Chemical Society. 120: 13525-13526. DOI: 10.1021/Ja982990I |
0.542 |
|
| 1998 |
Obias HV, Lin Y, Murthy NN, Pidcock E, Solomon EI, Ralle M, Blackburn NJ, Neuhold YM, Zuberbuhler AD, Karlin KD. Peroxo-, oxo-, and hydroxo-bridged dicopper complexes: Observation of exogenous hydrocarbon substrate oxidation [3] Journal of the American Chemical Society. 120: 12960-12961. DOI: 10.1021/Ja981878H |
0.346 |
|
| 1998 |
Obias HV, Van Strijdonck GPF, Lee DH, Ralle M, Blackburn NJ, Karlin KD. Heterobinucleating ligand-induced structural and chemical variations in [(L)Fe(III)-O-Cu(II)]+ μ-oxo complexes [9] Journal of the American Chemical Society. 120: 9696-9697. DOI: 10.1021/Ja9810989 |
0.333 |
|
| 1998 |
Hay MT, Ang MC, Gamelin DR, Solomon EI, Antholine WE, Ralle M, Blackburn NJ, Massey PD, Wang X, Kwon AH, Lu Y. Spectroscopic Characterization of an Engineered Purple CuACenter in Azurin Inorganic Chemistry. 37: 191-198. DOI: 10.1021/Ic971232A |
0.398 |
|
| 1998 |
Blackburn NJ, Ralle M, Sanders D, Fee JA, De Vries S, Houser RP, Tolman WB, Hay MT, Lu Y. XAS Studies on the CuA Centers of Heme-Copper Oxidases and Loop-Directed Mutants of Azurin: Implications for Redox Reactivity Acs Symposium Series. 692: 241-259. |
0.381 |
|
| 1997 |
Bell J, Ash DE, Snyder LM, Kulathila R, Blackburn NJ, Merkler DJ. Structural and functional investigations on the role of zinc in bifunctional rat peptidylglycine α-amidating enzyme Biochemistry. 36: 16239-16246. PMID 9405058 DOI: 10.1021/Bi970903D |
0.426 |
|
| 1997 |
Blackburn NJ, De Vries S, Barr ME, Houser RP, Tolman WB, Sanders D, Fee JA. X-ray absorption studies on the mixed-valence and fully reduced forms of the soluble Cu(A) domains of cytochrome c oxidase Journal of the American Chemical Society. 119: 6135-6143. DOI: 10.1021/Ja970513E |
0.53 |
|
| 1996 |
Boswell JS, Reedy BJ, Kulathila R, Merkler D, Blackburn NJ. Structural investigations on the coordination environment of the active-site copper centers of recombinant bifunctional peptidylglycine alpha-amidating enzyme. Biochemistry. 35: 12241-50. PMID 8823157 DOI: 10.1021/Bi960742Y |
0.643 |
|
| 1996 |
Blackburn NJ, de Vries S, Scott RA, Fee J, Lu Y, Dennison C, Canters G. XAS studies of the CuAcenters of cytochromecoxidase: a unique binuclear copper cluster Acta Crystallographica Section a Foundations of Crystallography. 52: C70-C70. DOI: 10.1107/S0108767396096286 |
0.365 |
|
| 1996 |
Fox S, Nanthakumar A, Wikström M, Karlin KD, Blackburn NJ. XAS Structural Comparisons of Reversibly Interconvertible Oxo- and Hydroxo-Bridged Heme-Copper Oxidase Model Compounds Journal of the American Chemical Society. 118: 24-34. DOI: 10.1021/Ja951686B |
0.402 |
|
| 1996 |
Fox S, Nanthakumar A, Wikström M, Karlin KD, Blackburn NJ. XAS structural comparisons of reversibly interconvertible oxo- and hydroxo-bridged heme-copper oxidase model compounds Journal of the American Chemical Society. 118: 24-34. |
0.39 |
|
| 1995 |
Eipper BA, Quon AS, Mains RE, Boswell JS, Blackburn NJ. The catalytic core of peptidylglycine alpha-hydroxylating monooxygenase: investigation by site-directed mutagenesis, Cu X-ray absorption spectroscopy, and electron paramagnetic resonance. Biochemistry. 34: 2857-65. PMID 7893699 DOI: 10.1021/Bi00009A016 |
0.424 |
|
| 1995 |
Fann YC, Ahmed I, Blackburn NJ, Boswell JS, Verkhovskaya ML, Hoffman BM, Wikström M. Structure of CuB in the binuclear heme-copper center of the cytochrome aa3-type quinol oxidase from Bacillus subtilis: an ENDOR and EXAFS study. Biochemistry. 34: 10245-55. PMID 7640280 DOI: 10.1021/Bi00032A019 |
0.508 |
|
| 1995 |
Houser RP, Halfen JA, Young VG, Blackburn NJ, Tolman WB. Structural characterization of the first example of a bis(μ-thiolato)dicopper(II) complex. Relevance to proposals for the electron transfer sites in cytochrome c oxidase and nitrous oxide reductase Journal of the American Chemical Society. 117: 10745-10746. DOI: 10.1021/Ja00148A018 |
0.529 |
|
| 1995 |
Reedy BJ, Murthy NN, Karlin KD, Blackburn NJ. Isocyanides as Ligand-Directed Indicators of Cu(I) Coordination in Copper Proteins. Probing the Inequivalence of the Cu(I) Centers in Reduced Dopamine-.beta.-monooxygenase Journal of the American Chemical Society. 117: 9826-9831. DOI: 10.1021/Ja00144A007 |
0.62 |
|
| 1995 |
Reedy BJ, Murthy NN, Karlin KD, Blackburn NJ. Isocyanides as ligand-directed indicators of Cu(I) coordination in copper proteins. Probing the inequivalence of the Cu(I) centers in reduced dopamine-β-monooxygenase Journal of the American Chemical Society. 117: 9826-9831. |
0.533 |
|
| 1994 |
Blackburn NJ. Metal-metal bonding in biology: EXAFS evidence for a 2.5 Å copper-copper bond in the Cua center of cytochrome oxidase Biochemistry®. 33: 10401-10407. PMID 8068678 DOI: 10.1021/Bi00200A022 |
0.605 |
|
| 1994 |
Reedy BJ, Blackburn NJ. Preparation and characterization of half-apo dopamine-β-hydroxylase by selective removal of CuA. identification of a sulfur ligand at the dioxygen binding site by EXAFS and FTIR spectroscopy Journal of the American Chemical Society. 116: 1924-1931. DOI: 10.1021/Ja00084A037 |
0.626 |
|
| 1993 |
Sanyal I, Karlin KD, Strange RW, Blackburn NJ. Chemistry and structural studies on the dioxygen-binding copper-1,2-dimethylimidazole system Journal of the American Chemical Society. 115: 11259-11270. DOI: 10.1021/Ja00077A027 |
0.496 |
|
| 1993 |
Nanthakumar A, Fox S, Murthy NN, Karlin KD, Ravi N, Huynh BH, Orosz RD, Day EP, Hagen KS, Blackburn NJ. Oxo- and hydroxo-bridged (porphyrin)iron(III)-copper(II) species as cytochrome c oxidase models: acid-base interconversions and x-ray structure of the Fe(III)-(O2-)-Cu(II) complex Journal of the American Chemical Society. 115: 8513-8514. DOI: 10.1021/Ja00071A097 |
0.453 |
|
| 1993 |
Blackburn NJ, Strange RW, Carr RT, Benkovic SJ. X-ray absorption studies of the copper-dependent phenylalanine hydroxylase from Chromobacterium violaceum. Comparison of the copper coordination in oxidized and dithionite-reduced enzymes. [Erratum to document cited in CA117(5):43463e] Biochemistry. 32: 9262-9262. DOI: 10.1021/Bi00086A036 |
0.454 |
|
| 1993 |
Reedy BT, Zhao G, Blackburn NJ. Isocyanide complexes of copper(I) proteins Journal of Inorganic Biochemistry. 51: 285. DOI: 10.1016/0162-0134(93)85317-2 |
0.456 |
|
| 1993 |
Karlin KD, Gan Q, Nanthakumar A, Fox S, Ravi N, Huynh BH, Orosz RD, Day EP, Hagen KS, Blackburn NJ. Copper-O22 reactivity. Involvement of oxodicopper(II) in amine oxidations and reduction of O2 using porphyrin-iron(II) and copper(I) Journal of Inorganic Biochemistry. 51: 278. DOI: 10.1016/0162-0134(93)85310-5 |
0.409 |
|
| 1993 |
Sanyal I, Karlin KD, Strange RW, Blackburn NJ. Chemistry and structural studies on the dioxygen-binding copper-1,2-dimethylimidazole system Journal of the American Chemical Society. 115: 11259-11270. |
0.516 |
|
| 1993 |
Nanthakumar A, Fox S, Murthy NN, Karlin KD, Ravi N, Huynh BH, Orosz RD, Day EP, Hagen KS, Blackburn NJ. Oxo- and hydroxo-bridged (porphyrin)iron(III)-copper(II) species as cytochrome c oxidase models: Acid-base interconversions and X-ray structure of the Fe(III)-(O2-)-Cu(II) complex Journal of the American Chemical Society. 115: 8513-8514. |
0.35 |
|
| 1992 |
Blackburn NJ, Strange RW, Carr RT, Benkovic SJ. X-ray absorption studies of the Cu-dependent phenylalanine hydroxylase from Chromobacterium violaceum. Comparison of the copper coordination in oxidized and dithionite-reduced enzymes. Biochemistry. 31: 5298-303. PMID 1606153 DOI: 10.1021/Bi00138A008 |
0.586 |
|
| 1992 |
Han J, Blackburn NJ, Loehr TM. Identification of the Cyanide Stretching Frequency in the Cyano Derivative of Copper/Zinc-Superoxide Dismutase by Ir and Raman Spectroscopy Inorganic Chemistry. 31: 3223-3229. DOI: 10.1021/Ic00041A011 |
0.589 |
|
| 1992 |
Mahroof-Tahir M, Murthy NN, Karlin KD, Blackburn NJ, Shaikh SN, Zubieta J. New thermally stable hydroperoxo- and peroxo-copper complexes Inorganic Chemistry. 31: 3001-3003. DOI: 10.1021/Ic00040A003 |
0.417 |
|
| 1992 |
Blackburn NJ, Reedy B, Zhou E, Carr R, Benkovic SJ. Chemistry and spectroscopy of copper monooxygenases Journal of Inorganic Biochemistry. 47: 8. DOI: 10.1016/0162-0134(92)84079-3 |
0.52 |
|
| 1992 |
Han J, Blackburn NJ, Loehr TM. Identification of the cyanide stretching frequency in the cyano derivative of Cu/Zn-superoxide dismutase by IR and Raman spectroscopy Inorganic Chemistry. 31: 3223-3229. |
0.508 |
|
| 1992 |
Mahroof-Tahir M, Murthy NN, Karlin KD, Blackburn NJ, Shaikh SN, Zubieta J. New thermally stable hydroperoxo- and peroxo-copper complexes Inorganic Chemistry. 31: 3001-3003. |
0.306 |
|
| 1991 |
Pettingill TM, Strange RW, Blackburn NJ. Carbonmonoxy dopamine β-hydroxylase. Structural characterization by Fourier transform infrared, fluorescence, and x-ray absorption spectroscopy Journal of Biological Chemistry. 266: 16996-17003. PMID 1894598 |
0.461 |
|
| 1991 |
Blackburn NJ, Hasnain SS, Pettingill TM, Strange RW. Copper K-extended X-ray absorption fine structure studies of oxidized and reduced dopamine β-hydroxylase. Confirmation of a sulfur ligand to copper(I) in the reduced enzyme Journal of Biological Chemistry. 266: 23120-23127. PMID 1744110 |
0.489 |
|
| 1991 |
Sanyal I, Strange RW, Blackburn NJ, Karlin KD. Formation of a Copper-Dioxygen Complex (cu2-o2) Using Simple Imidazole Ligands Journal of the American Chemical Society. 113: 4692-4693. DOI: 10.1021/Ja00012A054 |
0.561 |
|
| 1991 |
Sanyal I, Strange RW, Blackburn NJ, Karlin KD. Formation of a Copper-Dioxygen Complex (Cu2-O2) Using Simple Imidazole Ligands Journal of the American Chemical Society. 113: 4692-4693. |
0.48 |
|
| 1990 |
Blackburn NJ, Pettingill TM, Seagraves KS, Shigeta RT. Characterization of a carbon monoxide complex of reduced dopamine β-hydroxylase: Evidence for inequivalence of the Cu(I) centers Journal of Biological Chemistry. 265: 15383-15386. PMID 2394729 |
0.499 |
|
| 1989 |
Blackburn NJ, Strange RW, Reedijk J, Volbeda A, Farooq A, Karlin KD, Zubieta J. X-ray absorption edge spectroscopy of copper(I) complexes. Coordination geometry of copper(I) in the reduced forms of copper proteins and their derivatives with carbon monoxide Inorganic Chemistry. 28: 1349-1357. DOI: 10.1021/Ic00306A027 |
0.511 |
|
| 1989 |
Knowles PF, Strange RW, Blackburn NJ, Hasnain SS. EXAFS studies on pig plasma amine oxidase. A detailed structural analysis using the curved wave multiple scattering approach Journal of the American Chemical Society. 111: 102-107. |
0.312 |
|
| 1989 |
Blackburn NJ, Strange RW, Reedijk J, Volbeda A, Farooq A, Karlin KD, Zubieta J. X-ray absorption edge spectroscopy of copper(I) complexes. Coordination geometry of copper(I) in the reduced forms of copper proteins and their derivatives with carbon monoxide Inorganic Chemistry. 28: 1349-1357. |
0.546 |
|
| 1988 |
Blackburn NJ, Concannon M, Shahiyan SK, Mabbs FE, Collison D. Active site of dopamine β-hydroxylase. Comparison of enzyme derivatives containing four and eight copper atoms per tetramer using potentiometry and EPR spectroscopy Biochemistry. 27: 6001-6008. PMID 2847779 DOI: 10.1021/Bi00416A026 |
0.537 |
|
| 1988 |
Karlin KD, Ghosh P, Cruse RW, Farooq A, Gultneh Y, Jacobson RR, Blackburn NJ, Strange RW, Zubieta J. Dioxygen-copper reactivity: generation, characterization, and reactivity of a hydroperoxodicopper(II) complex Journal of the American Chemical Society. 110: 6769-6780. DOI: 10.1021/Ja00228A027 |
0.554 |
|
| 1988 |
Blackburn NJ, Strange RW, Farooq A, Haka MS, Karlin KD. X-ray absorption studies of three-coordinate dicopper(I) complexes and their dioxygen adducts Journal of the American Chemical Society. 110: 4263-4272. DOI: 10.1021/Ja00221A027 |
0.344 |
|
| 1988 |
Karlin KD, Ghosh P, Cruse RW, Farooq A, Gultneh Y, Jacobson RR, Blackburn NJ, Strange RW, Zubieta J. Dioxygen-copper reactivity: Generation, characterization, and reactivity of a hydroperoxo-dicopper(II) complex Journal of the American Chemical Society. 110: 6769-6780. |
0.339 |
|
| 1987 |
Blackburn NJ, Strange RW, McFadden LM, Hasnain SS. Anion binding to bovine erythrocyte superoxide dismutase studied by X-ray absorption spectroscopy. A detailed structural analysis of the native enzyme and the azido and cyano derivatives using a multiple-scattering approach Journal of the American Chemical Society. 109: 7162-7170. DOI: 10.1021/Ja00257A043 |
0.391 |
|
| 1987 |
Strange RW, Blackburn NJ, Knowles PF, Hasnain SS. X-ray absorption spectroscopy of metal-histidine coordination in metalloproteins. Exact simulation of the EXAFS of tetrakis(imidazole)copper(II) nitrate and other copper-imidazole complexes by the use of a multiple-scattering treatment Journal of the American Chemical Society. 109: 7157-7162. DOI: 10.1021/Ja00257A042 |
0.474 |
|
| 1987 |
Blackburn NJ, Strange RW, Cruse RW, Karlin KD. Dioxygen-copper reactivity: EXAFS studies of a peroxo-dicopper(II) complex Journal of the American Chemical Society. 109: 1235-1237. DOI: 10.1021/Ja00238A037 |
0.463 |
|
| 1987 |
Blackburn NJ, Strange RW, Cruse RW, Karlin KD. Dioxygen-copper reactivity: EXAFS studies of a peroxo-dicopper(II) complex Journal of the American Chemical Society. 109: 1235-1237. |
0.362 |
|
| 1986 |
HASNAIN SS, ALAGNA L, BLACKBURN NJ, STRANGE RW. EXAFS AND XANES OF SUPEROXIDE DISMUTASE : A COPPER PROTEIN Le Journal De Physique Colloques. 47: C8-1129-C8-1136. DOI: 10.1051/JPHYSCOL:19868220 |
0.372 |
|
| 1984 |
Blackburn NJ, Hasnain SS, Binsted N, Diakun GP, Garner CD, Knowles PF. An extended-X-ray-absorption-fine-structure study of bovine erythrocyte superoxide dismutase in aqueous solution. Direct evidence for three-co-ordinate Cu(I) in reduced enzyme. The Biochemical Journal. 219: 985-90. PMID 6743256 DOI: 10.1042/Bj2190985 |
0.522 |
|
| 1984 |
Hasnain SS, Diakun GP, Knowles PF, Binsted N, Garner CD, Blackburn NJ. Direct structural information for the copper site of dopamine beta-mono-oxygenase obtained by using extended X-ray-absorption fine structure. The Biochemical Journal. 221: 545-8. PMID 6477480 DOI: 10.1042/Bj2210545 |
0.405 |
|
| 1984 |
Blackburn NJ, Collison D, Sutton J, Mabbs FE. Kinetic and e.p.r. studies of cyanide and azide binding to the copper sites of dopamine (3,4-dihydroxyphenethylamine) beta-mono-oxygenase Biochemical Journal. 220: 447-454. PMID 6331417 |
0.421 |
|
| 1983 |
Blackburn NJ, Hasnain SS, Diakun GP, Knowles PF, Binsted N, Garner CD. An extended X-ray-absorption-fine-structure study of the copper and zinc sites of freeze-dried bovine superoxide dismutase. The Biochemical Journal. 213: 765-8. PMID 6615458 DOI: 10.1042/Bj2130765 |
0.505 |
|
| 1983 |
Ross I, Binstead N, Blackburn NJ, Bremner I, Diakun GP, Hasnain SS, Knowles PF, Vašák M, Garner C. EXAFS studies of copper and zinc in metallothionein and bovine superoxide dismutase Inorganica Chimica Acta. 79: 89-90. DOI: 10.1016/S0020-1693(00)95122-3 |
0.435 |
|
| 1982 |
Jameson RF, Blackburn NJ. The copper-catalysed oxidation of ascorbic acid by dioxygen. Part 4. The effect of chloride ions on the kinetics and mechanism Journal of the Chemical Society, Dalton Transactions. 9-13. DOI: 10.1039/Dt9820000009 |
0.405 |
|
| 1981 |
HASNAIN SS, BATMANIAN S, BLACKBURN NJ, BORDAS J, DIAKUN GP, GARNER CD, KNOWLES PF, MILLER RM. A study of the copper and zinc sites in native, high-pH, azide- and cyanide-bound forms of superoxide dismutase by X-ray-absorption spectroscopy Biochemical Society Transactions. 9: 444-444. DOI: 10.1042/bst0090444a |
0.34 |
|
| 1976 |
Jameson RF, Blackburn NJ. Role of copper dimers and the participation of copper(III) in the copper-catalysed autoxidation of ascorbic acid. Part II. Kinetics and mechanism in 0.100 mol dm-3 potassium nitrate Journal of the Chemical Society, Dalton Transactions. 534-541. DOI: 10.1039/Dt9760000534 |
0.578 |
|
| 1976 |
Jameson RF, Blackburn NJ. Role of copper dimers and the participation of copper(III) in the copper-catalysed autoxidation of ascorbic acid. Part III. Kinetics and mechanism in 0.100 mol dm-3 potassium chloride Journal of the Chemical Society, Dalton Transactions. 1596-1602. DOI: 10.1002/Chin.197621125 |
0.479 |
|
| 1975 |
Jameson RF, Blackburn NJ. The role of CuCu dinuclear complexes in the oxidation of ascorbic acid by O2 a model for copper-oxidase activity Journal of Inorganic and Nuclear Chemistry. 37: 809-814. DOI: 10.1016/0022-1902(75)80544-6 |
0.419 |
|
| Show low-probability matches. |