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Melvin Y. Okamura

Affiliations:

Physics

University of California, San Diego, La Jolla, CA

Area:

primary processes of photosynthesis

Website:

http://edrf.ucsd.edu/fac_staff/fac_profile/faculty_description.php?person_id=170

Google:

"Melvin Y. Okamura"

Bio:

http://www-physics.ucsd.edu/~raifeher/
Melvin Okamura is a Professor Emeritus of Biophysics at the University of California-San Diego. His main interests are the use of physical techniques and theories to unravel the primary processes of photosynthesis. He was the recipient of the National Institute of Health Career Development Award. He received his PhD in Biophysics from Northwestern University.
Dr. Okamura received his PhD in Physical Chemistry in 1970 from Northwestern University under Irving klotz studying the oxygen carrying iron protein, hemerythrin. He went to the Physics Department at the University of California, San Diego where he studied reaction centers from photosynthetic bacteria with George Feher. He has studied electron transfer and proton transfer reactions in reaction centers using spectroscopy, site directed mutation and structural techniques.

Mean distance: 10.81

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Parents

Irving M. Klotz	grad student	1970	Northwestern
(The nature of iron in hemerythrin)

Children

Collaborators

George Feher	collaborator		UCSD
(reaction centers from photosynthetic bacteria)

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Publications

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Okamura MY, Lubitz W, Allen JP. (2018) Remembering George Feher (1924-2017). Photosynthesis Research
Okamura M. (2013) George Feher: a pioneer in reaction center research. Photosynthesis Research. 120: 29-42
Flores M, Okamura MY, Niklas J, et al. (2012) Pulse Q-band EPR and ENDOR spectroscopies of the photochemically generated monoprotonated benzosemiquinone radical in frozen alcoholic solution. The Journal of Physical Chemistry. B. 116: 8890-900
Flores M, Savitsky A, Paddock ML, et al. (2010) Electron-nuclear and electron-electron double resonance spectroscopies show that the primary quinone acceptor QA in reaction centers from photosynthetic bacteria Rhodobacter sphaeroides remains in the same orientation upon light-induced reduction. The Journal of Physical Chemistry. B. 114: 16894-901
Paddock ML, Flores M, Isaacson R, et al. (2010) EPR and ENDOR Investigation of Rhodosemiquinone in Bacterial Reaction Centers Formed by B-Branch Electron Transfer. Applied Magnetic Resonance. 37: 39
Flores M, Isaacson R, Shepherd J, et al. (2010) Endor Spectrum of the Protonated Rhodosemiquinone in Bacterial Reaction Centers Biophysical Journal. 98: 173a
Abresch EC, Gong XM, Paddock ML, et al. (2009) Electron transfer from cytochrome c2 to the reaction center: A transition state model for ionic strength effects due to neutral mutations Biochemistry. 48: 11390-11398
Iwata T, Paddock ML, Okamura MY, et al. (2009) Identification of FTIR bands due to internal water molecules around the quinone binding sites in the reaction center from rhodobacter sphaeroides Biochemistry. 48: 1220-1229
Watanabe A, Iwata T, Paddock ML, et al. (2009) 3TP2-01 FTIR study of metal-replaced bacterial photosynthetic reaction center.(The 47th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 49: S60
Watanabe A, Iwata T, Paddock ML, et al. (2009) 3P-225 FTIR study of metal-replaced bacterial photosynthetic reaction center.(Photobiology:Photosynthesis,Oral Presentations,The 47th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 49: S189