| Year |
Citation |
Score |
| 2023 |
Schmidt A, Kalms J, Lorent C, Katz S, Frielingsdorf S, Evans RM, Fritsch J, Siebert E, Teutloff C, Armstrong FA, Zebger I, Lenz O, Scheerer P. Stepwise conversion of the Cys[4Fe-3S] to a Cys[4Fe-4S] cluster and its impact on the oxygen tolerance of [NiFe]-hydrogenase. Chemical Science. 14: 11105-11120. PMID 37860641 DOI: 10.1039/d3sc03739h |
0.368 |
|
| 2023 |
Evans RM, Beaton SE, Rodriguez Macia P, Pang Y, Wong KL, Kertess L, Myers WK, Bjornsson R, Ash PA, Vincent KA, Carr SB, Armstrong FA. Comprehensive structural, infrared spectroscopic and kinetic investigations of the roles of the active-site arginine in bidirectional hydrogen activation by the [NiFe]-hydrogenase 'Hyd-2' from . Chemical Science. 14: 8531-8551. PMID 37592998 DOI: 10.1039/d2sc05641k |
0.809 |
|
| 2022 |
Herold RA, Reinbold R, Schofield CJ, Armstrong FA. NADP(H)-dependent biocatalysis without adding NADP(H). Proceedings of the National Academy of Sciences of the United States of America. 120: e2214123120. PMID 36574703 DOI: 10.1073/pnas.2214123120 |
0.403 |
|
| 2022 |
Armstrong FA, Cheng B, Herold RA, Megarity CF, Siritanaratkul B. From Protein Film Electrochemistry to Nanoconfined Enzyme Cascades and the Electrochemical Leaf. Chemical Reviews. PMID 36573907 DOI: 10.1021/acs.chemrev.2c00397 |
0.825 |
|
| 2022 |
Cheng B, Heath RS, Turner NJ, Armstrong FA, Megarity CF. Deracemisation and stereoinversion by a nanoconfined bidirectional enzyme cascade: dual control by electrochemistry and selective metal ion activation. Chemical Communications (Cambridge, England). PMID 36178369 DOI: 10.1039/d2cc03638j |
0.302 |
|
| 2021 |
Ash PA, Kendall-Price SET, Evans RM, Carr SB, Brasnett AR, Morra S, Rowbotham JS, Hidalgo R, Healy AJ, Cinque G, Frogley MD, Armstrong FA, Vincent KA. The crystalline state as a dynamic system: IR microspectroscopy under electrochemical control for a [NiFe] hydrogenase. Chemical Science. 12: 12959-12970. PMID 34745526 DOI: 10.1039/d1sc01734a |
0.782 |
|
| 2021 |
Armstrong FA. Some fundamental insights into biological redox catalysis from the electrochemical characteristics of enzymes attached directly to electrodes. Electrochimica Acta. 390: 138836. PMID 34511630 DOI: 10.1016/j.electacta.2021.138836 |
0.301 |
|
| 2021 |
Herold RA, Reinbold R, Megarity CF, Abboud MI, Schofield CJ, Armstrong FA. Exploiting Electrode Nanoconfinement to Investigate the Catalytic Properties of Isocitrate Dehydrogenase (IDH1) and a Cancer-Associated Variant. The Journal of Physical Chemistry Letters. 12: 6095-6101. PMID 34170697 DOI: 10.1021/acs.jpclett.1c01517 |
0.311 |
|
| 2021 |
Evans RM, Krahn N, Murphy BJ, Lee H, Armstrong FA, Söll D. Selective cysteine-to-selenocysteine changes in a [NiFe]-hydrogenase confirm a special position for catalysis and oxygen tolerance. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 33753519 DOI: 10.1073/pnas.2100921118 |
0.399 |
|
| 2021 |
Morello G, Megarity CF, Armstrong FA. The power of electrified nanoconfinement for energising, controlling and observing long enzyme cascades. Nature Communications. 12: 340. PMID 33436601 DOI: 10.1038/s41467-020-20403-w |
0.302 |
|
| 2020 |
Cheng B, Wan L, Armstrong FA. Progress in Scaling up and Streamlining a Nanoconfined, Enzyme-Catalyzed Electrochemical Nicotinamide Recycling System for Biocatalytic Synthesis. Chemelectrochem. 7: 4672-4678. PMID 33381377 DOI: 10.1002/celc.202001166 |
0.339 |
|
| 2020 |
Megarity CF, Siritanaratkul B, Herold RA, Morello G, Armstrong FA. Electron flow between the worlds of Marcus and Warburg. The Journal of Chemical Physics. 153: 225101. PMID 33317312 DOI: 10.1063/5.0024701 |
0.797 |
|
| 2020 |
Lampret O, Duan J, Hofmann E, Winkler M, Armstrong FA, Happe T. The roles of long-range proton-coupled electron transfer in the directionality and efficiency of [FeFe]-hydrogenases. Proceedings of the National Academy of Sciences of the United States of America. PMID 32796105 DOI: 10.1073/Pnas.2007090117 |
0.331 |
|
| 2020 |
Zhang L, Morello G, Carr SB, Armstrong FA. Aerobic Photocatalytic H2 Production by a [NiFe] hydrogenase Engineered to Place a Silver Nanocluster in the Electron Relay. Journal of the American Chemical Society. PMID 32579353 DOI: 10.1021/jacs.0c04302 |
0.391 |
|
| 2019 |
Megarity C, Siritanaratkul B, Heath R, Wan L, Morello G, Fitzpatrick S, Booth R, Sills A, Robertson A, Warner J, Turner N, Armstrong FA. Electrocatalytic Volleyball: Rapid Nanoconfined Nicotinamide Cycling for Organic Synthesis in Electrode Pores. Angewandte Chemie (International Ed. in English). PMID 30633837 DOI: 10.1002/anie.201814370 |
0.802 |
|
| 2018 |
Evans RM, Siritanaratkul B, Megarity CF, Pandey K, Esterle TF, Badiani S, Armstrong FA. The value of enzymes in solar fuels research - efficient electrocatalysts through evolution. Chemical Society Reviews. PMID 30426997 DOI: 10.1039/c8cs00546j |
0.814 |
|
| 2018 |
Evans RM, Ash PA, Beaton SE, Brooke EJ, Vincent KA, Carr SB, Armstrong FA. Mechanistic Exploitation of a Self-Repairing, Blocked Proton Transfer Pathway in an O-Tolerant [NiFe]-Hydrogenase. Journal of the American Chemical Society. PMID 30070475 DOI: 10.1021/jacs.8b04798 |
0.823 |
|
| 2018 |
Volbeda A, Mouesca JM, Darnault C, Roessler MM, Parkin A, Armstrong FA, Fontecilla-Camps JC. X-ray structural, functional and computational studies of the O-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe-4S] cluster. Chemical Communications (Cambridge, England). PMID 29888350 DOI: 10.1039/C8Cc02896F |
0.793 |
|
| 2018 |
Armstrong FA, Evans RM, Megarity CF. Protein Film Electrochemistry of Iron-Sulfur Enzymes. Methods in Enzymology. 599: 387-407. PMID 29746247 DOI: 10.1016/bs.mie.2017.11.001 |
0.334 |
|
| 2018 |
Wan L, Megarity CF, Siritanaratkul B, Armstrong FA. A hydrogen fuel cell for rapid, enzyme-catalysed organic synthesis with continuous monitoring. Chemical Communications (Cambridge, England). PMID 29319070 DOI: 10.1039/c7cc08859k |
0.807 |
|
| 2017 |
Siritanaratkul B, Megarity CF, Roberts TG, Samuels TOM, Winkler M, Warner JH, Happe T, Armstrong FA. Transfer of photosynthetic NADP/NADPH recycling activity to a porous metal oxide for highly specific, electrochemically-driven organic synthesis. Chemical Science. 8: 4579-4586. PMID 30155220 DOI: 10.1039/c7sc00850c |
0.812 |
|
| 2017 |
Ash PA, Carr SB, Reeve HA, Skorupskaitė A, Rowbotham JS, Shutt R, Frogley MD, Evans RM, Cinque G, Armstrong FA, Vincent KA. Generating single metalloprotein crystals in well-defined redox states: electrochemical control combined with infrared imaging of a NiFe hydrogenase crystal. Chemical Communications (Cambridge, England). PMID 28504793 DOI: 10.1039/c7cc02591b |
0.553 |
|
| 2017 |
Pandey K, Islam ST, Happe T, Armstrong FA. Frequency and potential dependence of reversible electrocatalytic hydrogen interconversion by [FeFe]-hydrogenases. Proceedings of the National Academy of Sciences of the United States of America. PMID 28348243 DOI: 10.1073/pnas.1619961114 |
0.371 |
|
| 2016 |
Brooke EJ, Evans RM, Islam ST, Roberts GM, Wehlin SA, Carr SB, Phillips SE, Armstrong FA. Importance of the Active Site "Canopy" Residues in an O2-Tolerant [NiFe]-Hydrogenase. Biochemistry. PMID 28001048 DOI: 10.1021/acs.biochem.6b00868 |
0.36 |
|
| 2016 |
Megarity CF, Esselborn J, Hexter SV, Wittkamp F, Apfel UP, Happe T, Armstrong FA. Electrochemical Investigations of the Mechanism of Assembly of the Active-site H-Cluster of [FeFe]-hydrogenases. Journal of the American Chemical Society. PMID 27776209 DOI: 10.1021/Jacs.6B09366 |
0.32 |
|
| 2016 |
Armstrong FA, Evans RM, Hexter SV, Murphy BJ, Roessler MM, Wulff P. Guiding Principles of Hydrogenase Catalysis Instigated and Clarified by Protein Film Electrochemistry. Accounts of Chemical Research. PMID 27104487 DOI: 10.1021/acs.accounts.6b00027 |
0.488 |
|
| 2016 |
Wulff P, Thomas C, Sargent F, Armstrong FA. How the oxygen tolerance of a [NiFe]-hydrogenase depends on quaternary structure. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 26861789 DOI: 10.1007/s00775-015-1327-6 |
0.356 |
|
| 2015 |
Kelly CL, Pinske C, Murphy BJ, Parkin A, Armstrong F, Palmer T, Sargent F. Integration of an [FeFe]-hydrogenase into the anaerobic metabolism of Escherichia coli. Biotechnology Reports (Amsterdam, Netherlands). 8: 94-104. PMID 26839796 DOI: 10.1016/J.Btre.2015.10.002 |
0.782 |
|
| 2015 |
Wang VC, Islam ST, Can M, Ragsdale SW, Armstrong FA. Investigations by Protein Film Electrochemistry of Alternative Reactions of Nickel-Containing Carbon Monoxide Dehydrogenase. The Journal of Physical Chemistry. B. PMID 26176986 DOI: 10.1021/Acs.Jpcb.5B03098 |
0.339 |
|
| 2015 |
Murphy BJ, Hidalgo R, Roessler MM, Evans RM, Ash PA, Myers WK, Vincent KA, Armstrong FA. Discovery of Dark pH-Dependent H(+) Migration in a [NiFe]-Hydrogenase and Its Mechanistic Relevance: Mobilizing the Hydrido Ligand of the Ni-C Intermediate. Journal of the American Chemical Society. PMID 26103582 DOI: 10.1021/jacs.5b03182 |
0.791 |
|
| 2015 |
Bachmeier A, Esselborn J, Hexter SV, Krämer T, Klein K, Happe T, McGrady JE, Myers WK, Armstrong FA. How Formaldehyde Inhibits Hydrogen Evolution by [FeFe]-Hydrogenases: Determination by ¹³C ENDOR of Direct Fe-C Coordination and Order of Electron and Proton Transfers. Journal of the American Chemical Society. 137: 5381-9. PMID 25871921 DOI: 10.1021/ja513074m |
0.335 |
|
| 2015 |
Bachmeier A, Armstrong F. Solar-driven proton and carbon dioxide reduction to fuels—lessons from metalloenzymes. Current Opinion in Chemical Biology. 25: 141-51. PMID 25621455 DOI: 10.1016/J.Cbpa.2015.01.001 |
0.37 |
|
| 2015 |
Sigfridsson KG, Leidel N, Sanganas O, Chernev P, Lenz O, Yoon KS, Nishihara H, Parkin A, Armstrong FA, Dementin S, Rousset M, De Lacey AL, Haumann M. Structural differences of oxidized iron-sulfur and nickel-iron cofactors in O2-tolerant and O2-sensitive hydrogenases studied by X-ray absorption spectroscopy. Biochimica Et Biophysica Acta. 1847: 162-70. PMID 25316302 DOI: 10.1016/J.Bbabio.2014.06.011 |
0.787 |
|
| 2014 |
Hexter SV, Chung MW, Vincent KA, Armstrong FA. Unusual reaction of [NiFe]-hydrogenases with cyanide. Journal of the American Chemical Society. 136: 10470-7. PMID 25003708 DOI: 10.1021/ja504942h |
0.667 |
|
| 2014 |
Wulff P, Day CC, Sargent F, Armstrong FA. How oxygen reacts with oxygen-tolerant respiratory [NiFe]-hydrogenases. Proceedings of the National Academy of Sciences of the United States of America. 111: 6606-11. PMID 24715724 DOI: 10.1073/pnas.1322393111 |
0.359 |
|
| 2014 |
Evans RM, Armstrong FA. Electrochemistry of metalloproteins: protein film electrochemistry for the study of E. coli [NiFe]-hydrogenase-1. Methods in Molecular Biology (Clifton, N.J.). 1122: 73-94. PMID 24639254 DOI: 10.1007/978-1-62703-794-5_6 |
0.33 |
|
| 2014 |
Hexter SV, Esterle TF, Armstrong FA. A unified model for surface electrocatalysis based on observations with enzymes Physical Chemistry Chemical Physics. 16: 11822-11833. PMID 24556983 DOI: 10.1039/c3cp55230f |
0.321 |
|
| 2013 |
Bachmeier A, Wang VC, Woolerton TW, Bell S, Fontecilla-Camps JC, Can M, Ragsdale SW, Chaudhary YS, Armstrong FA. How light-harvesting semiconductors can alter the bias of reversible electrocatalysts in favor of H2 production and CO2 reduction. Journal of the American Chemical Society. 135: 15026-32. PMID 24070184 DOI: 10.1021/Ja4042675 |
0.758 |
|
| 2013 |
Wang VC, Ragsdale SW, Armstrong FA. Investigations of two bidirectional carbon monoxide dehydrogenases from Carboxydothermus hydrogenoformans by protein film electrochemistry. Chembiochem : a European Journal of Chemical Biology. 14: 1845-51. PMID 24002936 DOI: 10.1002/Cbic.201300270 |
0.311 |
|
| 2013 |
Evans RM, Parkin A, Roessler MM, Murphy BJ, Adamson H, Lukey MJ, Sargent F, Volbeda A, Fontecilla-Camps JC, Armstrong FA. Principles of sustained enzymatic hydrogen oxidation in the presence of oxygen--the crucial influence of high potential Fe-S clusters in the electron relay of [NiFe]-hydrogenases. Journal of the American Chemical Society. 135: 2694-707. PMID 23398301 DOI: 10.1021/Ja311055D |
0.816 |
|
| 2013 |
Volbeda A, Darnault C, Parkin A, Sargent F, Armstrong FA, Fontecilla-Camps JC. Crystal structure of the O2-Tolerant membrane-bound hydrogenase 1 from escherichia coli in complex with its cognate cytochrome b Structure. 21: 184-190. PMID 23260654 DOI: 10.1016/J.Str.2012.11.010 |
0.791 |
|
| 2012 |
Hexter SV, Grey F, Happe T, Climent V, Armstrong FA. Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases Proceedings of the National Academy of Sciences of the United States of America. 109: 11516-11521. PMID 22802675 DOI: 10.1073/Pnas.1204770109 |
0.382 |
|
| 2012 |
Stevenson GP, Lee CY, Kennedy GF, Parkin A, Baker RE, Gillow K, Armstrong FA, Gavaghan DJ, Bond AM. Theoretical analysis of the two-electron transfer reaction and experimental studies with surface-confined cytochrome c peroxidase using large-amplitude fourier transformed AC Voltammetry Langmuir. 28: 9864-9877. PMID 22607123 DOI: 10.1021/La205037E |
0.774 |
|
| 2012 |
Foster CE, Krämer T, Wait AF, Parkin A, Jennings DP, Happe T, McGrady JE, Armstrong FA. Inhibition of [FeFe]-hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation. Journal of the American Chemical Society. 134: 7553-7. PMID 22512303 DOI: 10.1021/Ja302096R |
0.795 |
|
| 2012 |
Volbeda A, Amara P, Darnault C, Mouesca JM, Parkin A, Roessler MM, Armstrong FA, Fontecilla-Camps JC. X-ray crystallographic and computational studies of the O 2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli Proceedings of the National Academy of Sciences of the United States of America. 109: 5305-5310. PMID 22431599 DOI: 10.1073/Pnas.1119806109 |
0.801 |
|
| 2012 |
Chaudhary YS, Woolerton TW, Allen CS, Warner JH, Pierce E, Ragsdale SW, Armstrong FA. Visible light-driven CO2 reduction by enzyme coupled CdS nanocrystals. Chemical Communications (Cambridge, England). 48: 58-60. PMID 22083268 DOI: 10.1039/C1Cc16107E |
0.679 |
|
| 2012 |
Parkin A, Bowman L, Roessler MM, Davies RA, Palmer T, Armstrong FA, Sargent F. How Salmonella oxidises H(2) under aerobic conditions. Febs Letters. 586: 536-44. PMID 21827758 DOI: 10.1016/J.Febslet.2011.07.044 |
0.805 |
|
| 2012 |
Krishnan S, Armstrong FA. Order-of-magnitude enhancement of an enzymatic hydrogen-air fuel cell based on pyrenyl carbon nanostructures Chemical Science. 3: 1015-1023. DOI: 10.1039/C2Sc01103D |
0.6 |
|
| 2012 |
Woolerton TW, Sheard S, Chaudhary YS, Armstrong FA. Enzymes and bio-inspired electrocatalysts in solar fuel devices Energy and Environmental Science. 5: 7470-7490. DOI: 10.1039/C2Ee21471G |
0.703 |
|
| 2011 |
Lukey MJ, Roessler MM, Parkin A, Evans RM, Davies RA, Lenz O, Friedrich B, Sargent F, Armstrong FA. Oxygen-tolerant [NiFe]-hydrogenases: the individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster. Journal of the American Chemical Society. 133: 16881-92. PMID 21916508 DOI: 10.1021/Ja205393W |
0.803 |
|
| 2011 |
Armstrong FA, Hirst J. Reversibility and efficiency in electrocatalytic energy conversion and lessons from enzymes. Proceedings of the National Academy of Sciences of the United States of America. 108: 14049-54. PMID 21844379 DOI: 10.1073/pnas.1103697108 |
0.334 |
|
| 2011 |
Reisner E, Armstrong FA. A TiO₂ nanoparticle system for sacrificial solar H₂ production prepared by rational combination of a hydrogenase with a ruthenium photosensitizer. Methods in Molecular Biology (Clifton, N.J.). 743: 107-17. PMID 21553186 DOI: 10.1007/978-1-61779-132-1_9 |
0.548 |
|
| 2011 |
Goris T, Wait AF, Saggu M, Fritsch J, Heidary N, Stein M, Zebger I, Lendzian F, Armstrong FA, Friedrich B, Lenz O. A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase. Nature Chemical Biology. 7: 310-8. PMID 21390036 DOI: 10.1038/Nchembio.555 |
0.624 |
|
| 2011 |
Wait AF, Brandmayr C, Stripp ST, Cavazza C, Fontecilla-Camps JC, Happe T, Armstrong FA. Formaldehyde--a rapid and reversible inhibitor of hydrogen production by [FeFe]-hydrogenases. Journal of the American Chemical Society. 133: 1282-5. PMID 21204519 DOI: 10.1021/ja110103p |
0.385 |
|
| 2011 |
Lee CY, Stevenson GP, Parkin A, Roessler MM, Baker RE, Gillow K, Gavaghan DJ, Armstrong FA, Bond AM. Theoretical and experimental investigation of surface-confined two-center metalloproteins by large-amplitude Fourier transformed ac voltammetry Journal of Electroanalytical Chemistry. 656: 293-303. DOI: 10.1016/J.Jelechem.2010.08.012 |
0.781 |
|
| 2010 |
Cracknell JA, Friedrich B, Armstrong FA. Gas pressure effects on the rates of catalytic H(2) oxidation by hydrogenases. Chemical Communications (Cambridge, England). 46: 8463-5. PMID 20922264 DOI: 10.1039/C0Cc03292A |
0.573 |
|
| 2010 |
Dos Santos L, Climent V, Blanford CF, Armstrong FA. Mechanistic studies of the 'blue' Cu enzyme, bilirubin oxidase, as a highly efficient electrocatalyst for the oxygen reduction reaction. Physical Chemistry Chemical Physics : Pccp. 12: 13962-74. PMID 20852807 DOI: 10.1039/C0Cp00018C |
0.357 |
|
| 2010 |
Danyal K, Inglet BS, Vincent KA, Barney BM, Hoffman BM, Armstrong FA, Dean DR, Seefeldt LC. Uncoupling nitrogenase: catalytic reduction of hydrazine to ammonia by a MoFe protein in the absence of Fe protein-ATP. Journal of the American Chemical Society. 132: 13197-9. PMID 20812745 DOI: 10.1021/Ja1067178 |
0.623 |
|
| 2010 |
Woolerton TW, Sheard S, Reisner E, Pierce E, Ragsdale SW, Armstrong FA. Efficient and clean photoreduction of CO(2) to CO by enzyme-modified TiO(2) nanoparticles using visible light. Journal of the American Chemical Society. 132: 2132-3. PMID 20121138 DOI: 10.1021/Ja910091Z |
0.489 |
|
| 2010 |
Rodgers CJ, Blanford CF, Giddens SR, Skamnioti P, Armstrong FA, Gurr SJ. Designer laccases: a vogue for high-potential fungal enzymes? Trends in Biotechnology. 28: 63-72. PMID 19963293 DOI: 10.1016/J.Tibtech.2009.11.001 |
0.3 |
|
| 2010 |
Lukey MJ, Parkin A, Roessler MM, Murphy BJ, Harmer J, Palmer T, Sargent F, Armstrong FA. How Escherichia coli is equipped to oxidize hydrogen under different redox conditions. The Journal of Biological Chemistry. 285: 3928-38. PMID 19917611 DOI: 10.1074/Jbc.M109.067751 |
0.813 |
|
| 2010 |
Wait AF, Parkin A, Morley GM, Dos Santos L, Armstrong FA. Characteristics of enzyme-based hydrogen fuel cells using an oxygen-tolerant hydrogenase as the anodic catalyst Journal of Physical Chemistry C. 114: 12003-12009. DOI: 10.1021/Jp102616M |
0.799 |
|
| 2009 |
Cracknell JA, Wait AF, Lenz O, Friedrich B, Armstrong FA. A kinetic and thermodynamic understanding of O2 tolerance in [NiFe]-hydrogenases. Proceedings of the National Academy of Sciences of the United States of America. 106: 20681-6. PMID 19934053 DOI: 10.1073/Pnas.0905959106 |
0.621 |
|
| 2009 |
Reisner E, Powell DJ, Cavazza C, Fontecilla-Camps JC, Armstrong FA. Visible light-driven H(2) production by hydrogenases attached to dye-sensitized TiO(2) nanoparticles. Journal of the American Chemical Society. 131: 18457-66. PMID 19928857 DOI: 10.1021/Ja907923R |
0.56 |
|
| 2009 |
Goldet G, Brandmayr C, Stripp ST, Happe T, Cavazza C, Fontecilla-Camps JC, Armstrong FA. Electrochemical kinetic investigations of the reactions of [FeFe]-hydrogenases with carbon monoxide and oxygen: comparing the importance of gas tunnels and active-site electronic/redox effects. Journal of the American Chemical Society. 131: 14979-89. PMID 19824734 DOI: 10.1021/ja905388j |
0.368 |
|
| 2009 |
Lazarus O, Woolerton TW, Parkin A, Lukey MJ, Reisner E, Seravalli J, Pierce E, Ragsdale SW, Sargent F, Armstrong FA. Water-gas shift reaction catalyzed by redox enzymes on conducting graphite platelets. Journal of the American Chemical Society. 131: 14154-5. PMID 19807170 DOI: 10.1021/Ja905797W |
0.805 |
|
| 2009 |
Stripp ST, Goldet G, Brandmayr C, Sanganas O, Vincent KA, Haumann M, Armstrong FA, Happe T. How oxygen attacks [FeFe] hydrogenases from photosynthetic organisms. Proceedings of the National Academy of Sciences of the United States of America. 106: 17331-6. PMID 19805068 DOI: 10.1073/pnas.0905343106 |
0.651 |
|
| 2009 |
Armstrong FA. Dynamic electrochemical experiments on hydrogenases. Photosynthesis Research. 102: 541-50. PMID 19455401 DOI: 10.1007/s11120-009-9428-0 |
0.324 |
|
| 2009 |
Reisner E, Fontecilla-Camps JC, Armstrong FA. Catalytic electrochemistry of a [NiFeSe]-hydrogenase on TiO2 and demonstration of its suitability for visible-light driven H2 production. Chemical Communications (Cambridge, England). 550-2. PMID 19283287 DOI: 10.1039/B817371K |
0.556 |
|
| 2009 |
Armstrong FA, Belsey NA, Cracknell JA, Goldet G, Parkin A, Reisner E, Vincent KA, Wait AF. Dynamic electrochemical investigations of hydrogen oxidation and production by enzymes and implications for future technology. Chemical Society Reviews. 38: 36-51. PMID 19088963 DOI: 10.1039/B801144N |
0.818 |
|
| 2009 |
Ludwig M, Cracknell JA, Vincent KA, Armstrong FA, Lenz O. Oxygen-tolerant H2 oxidation by membrane-bound [NiFe] hydrogenases of ralstonia species. Coping with low level H2 in air. The Journal of Biological Chemistry. 284: 465-77. PMID 18990688 DOI: 10.1074/jbc.M803676200 |
0.679 |
|
| 2008 |
Blanford CF, Foster CE, Heath RS, Armstrong FA. Efficient electrocatalytic oxygen reduction by the 'blue' copper oxidase, laccase, directly attached to chemically modified carbons. Faraday Discussions. 140: 319-35; discussion 4. PMID 19213324 DOI: 10.1039/B808939F |
0.33 |
|
| 2008 |
Parkin A, Goldet G, Cavazza C, Fontecilla-Camps JC, Armstrong FA. The difference a Se makes? Oxygen-tolerant hydrogen production by the [NiFeSe]-hydrogenase from Desulfomicrobium baculatum. Journal of the American Chemical Society. 130: 13410-6. PMID 18781742 DOI: 10.1021/Ja803657D |
0.803 |
|
| 2008 |
Goldet G, Wait AF, Cracknell JA, Vincent KA, Ludwig M, Lenz O, Friedrich B, Armstrong FA. Hydrogen production under aerobic conditions by membrane-bound hydrogenases from Ralstonia species. Journal of the American Chemical Society. 130: 11106-13. PMID 18661984 DOI: 10.1021/Ja8027668 |
0.751 |
|
| 2008 |
Cracknell JA, Vincent KA, Armstrong FA. Enzymes as working or inspirational electrocatalysts for fuel cells and electrolysis. Chemical Reviews. 108: 2439-61. PMID 18620369 DOI: 10.1021/cr0680639 |
0.61 |
|
| 2008 |
Cracknell JA, Vincent KA, Ludwig M, Lenz O, Friedrich B, Armstrong FA. Enzymatic oxidation of H2 in atmospheric O2: the electrochemistry of energy generation from trace H2 by aerobic microorganisms. Journal of the American Chemical Society. 130: 424-5. PMID 18088128 DOI: 10.1021/Ja078299+ |
0.758 |
|
| 2007 |
Vincent KA, Li X, Blanford CF, Belsey NA, Weiner JH, Armstrong FA. Enzymatic catalysis on conducting graphite particles. Nature Chemical Biology. 3: 761-2. PMID 17994012 DOI: 10.1038/Nchembio.2007.47 |
0.655 |
|
| 2007 |
Vincent KA, Parkin A, Armstrong FA. Investigating and exploiting the electrocatalytic properties of hydrogenases. Chemical Reviews. 107: 4366-413. PMID 17845060 DOI: 10.1021/cr050191u |
0.76 |
|
| 2007 |
Parkin A, Seravalli J, Vincent KA, Ragsdale SW, Armstrong FA. Rapid and efficient electrocatalytic CO2/CO interconversions by Carboxydothermus hydrogenoformans CO dehydrogenase I on an electrode. Journal of the American Chemical Society. 129: 10328-9. PMID 17672466 DOI: 10.1021/Ja073643O |
0.777 |
|
| 2007 |
Blanford CF, Heath RS, Armstrong FA. A stable electrode for high-potential, electrocatalytic O(2) reduction based on rational attachment of a blue copper oxidase to a graphite surface. Chemical Communications (Cambridge, England). 1710-2. PMID 17457416 DOI: 10.1039/B703114A |
0.314 |
|
| 2006 |
Parkin A, Cavazza C, Fontecilla-Camps JC, Armstrong FA. Electrochemical investigations of the interconversions between catalytic and inhibited states of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. Journal of the American Chemical Society. 128: 16808-15. PMID 17177431 DOI: 10.1021/Ja064425I |
0.815 |
|
| 2006 |
Vincent KA, Cracknell JA, Clark JR, Ludwig M, Lenz O, Friedrich B, Armstrong FA. Electricity from low-level H2 in still air--an ultimate test for an oxygen tolerant hydrogenase. Chemical Communications (Cambridge, England). 5033-5. PMID 17146518 DOI: 10.1039/B614272A |
0.75 |
|
| 2006 |
Vincent KA, Belsey NA, Lubitz W, Armstrong FA. Rapid and reversible reactions of [NiFe]-hydrogenases with sulfide. Journal of the American Chemical Society. 128: 7448-9. PMID 16756292 DOI: 10.1021/ja061732f |
0.68 |
|
| 2006 |
Pankhurst KL, Mowat CG, Rothery EL, Hudson JM, Jones AK, Miles CS, Walkinshaw MD, Armstrong FA, Reid GA, Chapman SK. A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina. The Journal of Biological Chemistry. 281: 20589-97. PMID 16699170 DOI: 10.1074/Jbc.M603077200 |
0.604 |
|
| 2005 |
Vincent KA, Parkin A, Lenz O, Albracht SP, Fontecilla-Camps JC, Cammack R, Friedrich B, Armstrong FA. Electrochemical definitions of O2 sensitivity and oxidative inactivation in hydrogenases. Journal of the American Chemical Society. 127: 18179-89. PMID 16366571 DOI: 10.1021/Ja055160V |
0.811 |
|
| 2005 |
Vincent KA, Cracknell JA, Lenz O, Zebger I, Friedrich B, Armstrong FA. Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levels. Proceedings of the National Academy of Sciences of the United States of America. 102: 16951-4. PMID 16260746 DOI: 10.1073/Pnas.0504499102 |
0.743 |
|
| 2005 |
Vincent KA, Cracknell JA, Parkin A, Armstrong FA. Hydrogen cycling by enzymes: electrocatalysis and implications for future energy technology. Dalton Transactions (Cambridge, England : 2003). 3397-403. PMID 16234917 DOI: 10.1039/B508520A |
0.829 |
|
| 2005 |
Armstrong FA, Albracht SP. [NiFe]-hydrogenases: spectroscopic and electrochemical definition of reactions and intermediates. Philosophical Transactions. Series a, Mathematical, Physical, and Engineering Sciences. 363: 937-54; discussion 1. PMID 15991402 DOI: 10.1098/Rsta.2004.1528 |
0.422 |
|
| 2005 |
Hudson JM, Heffron K, Kotlyar V, Sher Y, Maklashina E, Cecchini G, Armstrong FA. Electron transfer and catalytic control by the iron-sulfur clusters in a respiratory enzyme, E. coli fumarate reductase. Journal of the American Chemical Society. 127: 6977-89. PMID 15884941 DOI: 10.1021/ja043404q |
0.316 |
|
| 2005 |
Lamle SE, Albracht SP, Armstrong FA. The mechanism of activation of a [NiFe]-hydrogenase by electrons, hydrogen, and carbon monoxide. Journal of the American Chemical Society. 127: 6595-604. PMID 15869280 DOI: 10.1021/Ja0424934 |
0.4 |
|
| 2005 |
Vincent KA, Armstrong FA. Investigating metalloenzyme reactions using electrochemical sweeps and steps: fine control and measurements with reactants ranging from ions to gases. Inorganic Chemistry. 44: 798-809. PMID 15859247 |
0.655 |
|
| 2004 |
Lamle SE, Albracht SP, Armstrong FA. Electrochemical potential-step investigations of the aerobic interconversions of [NiFe]-hydrogenase from Allochromatium vinosum: insights into the puzzling difference between unready and ready oxidized inactive states. Journal of the American Chemical Society. 126: 14899-909. PMID 15535717 DOI: 10.1021/Ja047939V |
0.34 |
|
| 2004 |
Hoke KR, Cobb N, Armstrong FA, Hille R. Electrochemical studies of arsenite oxidase: an unusual example of a highly cooperative two-electron molybdenum center. Biochemistry. 43: 1667-74. PMID 14769044 DOI: 10.1021/Bi0357154 |
0.364 |
|
| 2004 |
Elliott SJ, Hoke KR, Heffron K, Palak M, Rothery RA, Weiner JH, Armstrong FA. Voltammetric studies of the catalytic mechanism of the respiratory nitrate reductase from Escherichia coli: how nitrate reduction and inhibition depend on the oxidation state of the active site. Biochemistry. 43: 799-807. PMID 14730985 DOI: 10.1021/Bi035869J |
0.536 |
|
| 2003 |
Vincent KA, Tilley GJ, Quammie NC, Streeter I, Burgess BK, Cheesman MR, Armstrong FA. Instantaneous, stoichiometric generation of powerfully reducing states of protein active sites using Eu(II) and polyaminocarboxylate ligands. Chemical Communications (Cambridge, England). 2590-1. PMID 14594295 |
0.606 |
|
| 2003 |
Léger C, Elliott SJ, Hoke KR, Jeuken LJ, Jones AK, Armstrong FA. Enzyme electrokinetics: using protein film voltammetry to investigate redox enzymes and their mechanisms. Biochemistry. 42: 8653-62. PMID 12873124 DOI: 10.1021/Bi034789C |
0.728 |
|
| 2003 |
Jones AK, Lamle SE, Pershad HR, Vincent KA, Albracht SP, Armstrong FA. Enzyme electrokinetics: electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase. Journal of the American Chemical Society. 125: 8505-14. PMID 12848556 DOI: 10.1021/Ja035296Y |
0.774 |
|
| 2003 |
Lamle SE, Vincent KA, Halliwell LM, Albracht SPJ, Armstrong FA. Hydrogenase on an electrode: A remarkable heterogeneous catalyst Journal of the Chemical Society. Dalton Transactions. 4152-4157. DOI: 10.1039/B306234C |
0.68 |
|
| 2003 |
Vincent KA, Kadodia SM, Armstrong FA, Gurr SJ. Electrochemical insights into inhibition of multi-copper oxidases Journal of Inorganic Biochemistry. 96: 244. DOI: 10.1016/S0162-0134(03)80795-X |
0.577 |
|
| 2003 |
Hoke KR, Elliott SJ, Armstrong FA. The effect of oxidation state on inhibition of nitrate reductase Journal of Inorganic Biochemistry. 96: 150. DOI: 10.1016/S0162-0134(03)80642-6 |
0.469 |
|
| 2002 |
Léger C, Jones AK, Roseboom W, Albracht SP, Armstrong FA. Enzyme electrokinetics: hydrogen evolution and oxidation by Allochromatium vinosum [NiFe]-hydrogenase. Biochemistry. 41: 15736-46. PMID 12501202 DOI: 10.1021/Bi026586E |
0.673 |
|
| 2002 |
Elliott SJ, McElhaney AE, Feng C, Enemark JH, Armstrong FA. A voltammetric study of interdomain electron transfer within sulfite oxidase. Journal of the American Chemical Society. 124: 11612-3. PMID 12296723 DOI: 10.1021/Ja027776F |
0.524 |
|
| 2002 |
Elliott SJ, Léger C, Pershad HR, Hirst J, Heffron K, Ginet N, Blasco F, Rothery RA, Weiner JH, Armstrong FA. Detection and interpretation of redox potential optima in the catalytic activity of enzymes. Biochimica Et Biophysica Acta. 1555: 54-9. PMID 12206891 DOI: 10.1016/S0005-2728(02)00254-2 |
0.555 |
|
| 2002 |
Jones AK, Sillery E, Albracht SP, Armstrong FA. Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst. Chemical Communications (Cambridge, England). 866-7. PMID 12123018 DOI: 10.1039/B201337A |
0.645 |
|
| 2002 |
Jeuken LJ, Jones AK, Chapman SK, Cecchini G, Armstrong FA. Electron-transfer mechanisms through biological redox chains in multicenter enzymes. Journal of the American Chemical Society. 124: 5702-13. PMID 12010043 DOI: 10.1021/ja012638w |
0.622 |
|
| 2002 |
Léger C, Jones AK, Albracht SPJ, Armstrong FA. Effect of a dispersion of interfacial electron transfer rates on steady state catalytic electron transport in [NiFe]-hydrogenase and other enzymes Journal of Physical Chemistry B. 106: 13058-13063. DOI: 10.1021/Jp0265687 |
0.654 |
|
| 2001 |
Bateman L, Léger C, Goodin DB, Armstrong FA. A distal histidine mutant (H52Q) of yeast cytochrome c peroxidase catalyzes the oxidation of H(2)O(2) instead of its reduction. Journal of the American Chemical Society. 123: 9260-3. PMID 11562206 DOI: 10.1021/ja0158612 |
0.385 |
|
| 2001 |
Léger C, Heffron K, Pershad HR, Maklashina E, Luna-Chavez C, Cecchini G, Ackrell BA, Armstrong FA. Enzyme electrokinetics: energetics of succinate oxidation by fumarate reductase and succinate dehydrogenase. Biochemistry. 40: 11234-45. PMID 11551223 DOI: 10.1021/bi010889b |
0.331 |
|
| 2001 |
Heffron K, Léger C, Rothery RA, Weiner JH, Armstrong FA. Determination of an optimal potential window for catalysis by E. coli dimethyl sulfoxide reductase and hypothesis on the role of Mo(V) in the reaction pathway. Biochemistry. 40: 3117-26. PMID 11258926 DOI: 10.1021/bi002452u |
0.37 |
|
| 2000 |
Canters GW, Kolczak U, Armstrong F, Jeuken LJ, Camba R, Sola M. The effect of pH and ligand exchange on the redox properties of blue copper proteins. Faraday Discussions. 205-20; discussion 2. PMID 11197479 DOI: 10.1039/B003822I |
0.33 |
|
| 2000 |
Armstrong FA, Camba R, Heering HA, Hirst J, Jeuken LJ, Jones AK, Léger C, McEvoy JP. Fast voltammetric studies of the kinetics and energetics of coupled electron-transfer reactions in proteins. Faraday Discussions. 191-203; discussion . PMID 11197478 DOI: 10.1039/B002290J |
0.616 |
|
| 2000 |
Jones AK, Camba R, Reid GA, Chapman SK, Armstrong FA. Interruption and time-resolution of catalysis by a flavoenzyme using fast scan protein film voltammetry [4] Journal of the American Chemical Society. 122: 6494-6495. DOI: 10.1021/ja000848n |
0.532 |
|
| 1999 |
Pershad HR, Duff JL, Heering HA, Duin EC, Albracht SP, Armstrong FA. Catalytic electron transport in Chromatium vinosum [NiFe]-hydrogenase: application of voltammetry in detecting redox-active centers and establishing that hydrogen oxidation is very fast even at potentials close to the reversible H+/H2 value. Biochemistry. 38: 8992-9. PMID 10413472 DOI: 10.1021/Bi990108V |
0.423 |
|
| 1999 |
Armstrong FA, Williams RJ. Thermodynamic influences on the fidelity of iron-sulphur cluster formation in proteins. Febs Letters. 451: 91-4. PMID 10371144 DOI: 10.1016/S0014-5793(99)00545-1 |
0.381 |
|
| 1996 |
Van Dyke BR, Saltman P, Armstrong FA. Control of myoglobin electron-transfer rates by the distal (nonbound) histidine residue Journal of the American Chemical Society. 118: 3490-3492. DOI: 10.1021/ja954181u |
0.355 |
|
| 1993 |
Sucheta A, Cammack R, Weiner J, Armstrong FA. Reversible electrochemistry of fumarate reductase immobilized on an electrode surface. Direct voltammetric observations of redox centers and their participation in rapid catalytic electron transport. Biochemistry. 32: 5455-65. PMID 8499449 DOI: 10.1021/bi00071a023 |
0.388 |
|
| 1993 |
Armstrong FA, Bond AM, Büchi FN, Hamnett A, Hill HA, Lannon AM, Lettington OC, Zoski CG. Electrocatalytic reduction of hydrogen peroxide at a stationary pyrolytic graphite electrode surface in the presence of cytochrome c peroxidase: a description based on a microelectrode array model for adsorbed enzyme molecules. The Analyst. 118: 973-8. PMID 8214607 DOI: 10.1039/An9931800973 |
0.559 |
|
| 1992 |
Sucheta A, Ackrell BA, Cochran B, Armstrong FA. Diode-like behaviour of a mitochondrial electron-transport enzyme. Nature. 356: 361-2. PMID 1549182 DOI: 10.1038/356361a0 |
0.338 |
|
| 1990 |
Armstrong FA, Butt JN, Govindaraju K, McGinnis J, Powls R, Sykes AG. Direct cyclic voltammetry of three ruthenium-modified electron-transfer proteins Inorganic Chemistry. 29: 4858-4862. DOI: 10.1021/ic00349a009 |
0.409 |
|
| 1989 |
Armstrong FA, Bond AM, Hill HAO, Oliver BN, Psalti ISM. Electrochemistry of cytochrome c, plastocyanin, and ferredoxin at edge- and basal-plane graphite electrodes interpreted via a model based on electron transfer at electroactive sites of microscopic dimensions in size Journal of the American Chemical Society. 111: 9185-9189. DOI: 10.1021/Ja00208A008 |
0.528 |
|
| 1989 |
Armstrong FA, Bond AM, Hill HAO, Psalti ISM, Zoski CG. A microscopic model of electron transfer at electroactive sites of molecular dimensions for reduction of cytochrome c at basal- and edge-plane graphite electrodes The Journal of Physical Chemistry. 93: 6485-6493. DOI: 10.1021/J100354A041 |
0.5 |
|
| 1988 |
Armstrong FA, Driscoll PC, Hill HA, Redfield C. Investigation of the function of plastocyanin by electrochemistry and nuclear-magnetic-resonance spectroscopy. Biochemical Society Transactions. 15: 767-72. PMID 3678593 DOI: 10.1042/bst0150767 |
0.392 |
|
| 1988 |
Armstrong FA, Hill HAO, Walton NJ. Direct electrochemistry of redox proteins Accounts of Chemical Research. 21: 407-413. DOI: 10.1021/ar00155a004 |
0.447 |
|
| 1987 |
Armstrong FA, Anthony Cox P, Hill HO, Lowe VJ, Nigel Oliver B. Metal ions and complexes as modulators of protein-interfacial electron transport at graphite electrodes Journal of Electroanalytical Chemistry and Interfacial Electrochemistry. 217: 331-366. DOI: 10.1016/0022-0728(87)80228-0 |
0.458 |
|
| 1986 |
ARMSTRONG FA, HILL HAO, OLIVER BN, WHITFORD D. Direct electrochemistry of the ‘blue’ copper protein plastocyanin Biochemical Society Transactions. 14: 44-45. DOI: 10.1042/bst0140044 |
0.411 |
|
| 1985 |
ARMSTRONG FA, HILL HAO, OLIVER BN, WHITFORD D. ChemInform Abstract: Direct Electrochemistry of the Photosynthetic Blue Copper Protein Plastocyanin. Electrostatic Promotion of Rapid Charge Transfer at an Edge-Oriented Pyrolytic Graphite Electrode Chemischer Informationsdienst. 16. DOI: 10.1002/chin.198530083 |
0.473 |
|
| 1984 |
Armstrong FA, Hill HAO, Oliver BN, Walton NJ. Direct electrochemistry of redox proteins at pyrolytic graphite electrodes Journal of the American Chemical Society. 106: 921-923. DOI: 10.1021/ja00316a015 |
0.487 |
|
| 1983 |
Armstrong F, Shaw RW, Beinert H. Cytochrome c oxidase. Time dependence of optical and EPR spectral changes related to the 'oxygen-pulsed' form. Biochimica Et Biophysica Acta. 722: 61-71. PMID 6297568 DOI: 10.1016/0005-2728(83)90157-3 |
0.539 |
|
| 1982 |
Armstrong FA, Sykes A. Preparation and properties of a soluble polymeric aquo ion of molybdenum(V) Polyhedron. 1: 109-111. DOI: 10.1016/S0277-5387(00)81077-3 |
0.421 |
|
| 1982 |
ARMSTRONG FA, SYKES AG. ChemInform Abstract: PREPARATION AND PROPERTIES OF A SOLUBLE POLYMERIC AQUO ION OF MOLYBDENUM(V) Chemischer Informationsdienst. 13. DOI: 10.1002/chin.198225038 |
0.318 |
|
| 1981 |
Petrou AL, Armstrong FA, Sykes A, Harrington PC, Wilkins RG. Kinetics of the equilibration of oxygen with monomeric and octameric hemerythrin from Themiste zostericola Biochimica Et Biophysica Acta (Bba) - Protein Structure. 670: 377-384. DOI: 10.1016/0005-2795(81)90110-0 |
0.354 |
|
| 1980 |
Armstrong FA, Henderson RA, Sykes AG. Kinetic studies on reactions of iron-sulfur proteins. 3. Oxidation of the reduced form of Clostridium pasteurianum 8-iron ferredoxin with inorganic complexes. Observation of single-stage kinetics for a difunctional protein reactant Journal of the American Chemical Society. 102: 6545-6551. DOI: 10.1021/Ja00541A026 |
0.405 |
|
| 1980 |
ARMSTRONG FA, HENDERSON RA, SYKES AG. ChemInform Abstract: KINETIC STUDIES ON REACTIONS OF IRON-SULFUR PROTEINS. 2. AN EXTENSION OF THE RANGE OF OXIDANTS IN THE REACTION OF REDUCED PARSLEY 2-FE FERREDOXIN AND IDENTIFICATION OF SPECIFIC BINDING SITES USING REDOX INACTIVE CR(NH3)63+ (AND CR(EN) Chemischer Informationsdienst. 11. DOI: 10.1002/chin.198007310 |
0.431 |
|
| 1979 |
Butler J, Henderson RA, Armstrong FA, Sykes AG. Mechanism of formation, spectrum and reactivity of half-reduced eight-iron Clostridium pasteurianum ferredoxin in pulse-radiolysis studies and the non-co-operativity of the four-iron clusters. The Biochemical Journal. 183: 471-4. PMID 534509 |
0.441 |
|
| 1979 |
Armstrong FA, Henderson RA, Sykes AG. Kinetic studies on reactions of iron-sulfur proteins. 2. An extension of the range of oxidants in the reaction of reduced parsley 2-Fe ferredoxin and identification of specific binding sites using redox inactive Cr(NH3)63+ (and Cr(en)33+) Journal of the American Chemical Society. 101: 6912-6917. DOI: 10.1021/Ja00517A021 |
0.43 |
|
| 1979 |
ARMSTRONG FA, SYKES AG. ChemInform Abstract: Kinetic Studies on Reactions of Iron-Sulfur Proteins. Part 1. Oxidation of Reduced Parsley (and Spinach) 2-Iron Ferredoxins with Co(NH3)6)3+ dl- and d-Co(en)3)3+, Co(NH3)5Cl)2+ , Co(NH3)5C2O4)+ Co(dmgH)2 (C6H5NH2)2)+, and Co(edta)-. E Chemischer Informationsdienst. 10. DOI: 10.1002/chin.197909279 |
0.407 |
|
| 1978 |
Armstrong FA, Sykes AG. Kinetic studies on reactions of iron-sulfur proteins. 1. Oxidation of reduced parsley (and spinach) 2-iron ferredoxins with Co(NH3)63+, dl- and d- Co(en)33+, Co(NH3)5Cl2+, Co(NH3)5C2O4+, Co(dmgH)2(C6H5NH2)2+, and Co(edta)-. Evidence for protein-complex association Journal of the American Chemical Society. 100: 7710-7715. DOI: 10.1021/Ja00492A045 |
0.403 |
|
| 1978 |
Armstrong FA, Shibahara T, Sykes AG. Effect of .mu.-sulfido ligands on substitution at molybdenum(V). A temperature-jump study of the 1:1 equilibration of thiocyanate with di-.mu.-sulfido-bis[aquooxalatooxomolybdenum(V)] Inorganic Chemistry. 17: 189-191. DOI: 10.1021/Ic50179A036 |
0.319 |
|
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