Photosynthetic reaction centre, Electron transfer, Photochemistry, Acceptor and Rhodobacter sphaeroides are his primary areas of study. His Photosynthetic reaction centre research incorporates themes from Proton-coupled electron transfer, Protonation, Stereochemistry and Photosystem. He interconnects Crystallography, Analytical chemistry, Recombination and Bacteriochlorophyll in the investigation of issues within Electron transfer.
His studies in Photochemistry integrate themes in fields like Photosynthesis, Physical chemistry and Active site. His study explores the link between Electron acceptor and topics such as Electron donor that cross with problems in Rhodopseudomonas spheroides and Photosynthetic bacteria. His Electron paramagnetic resonance research includes elements of Electronic structure and Atomic physics.
Melvin Y. Okamura mainly investigates Photosynthetic reaction centre, Electron transfer, Photochemistry, Rhodobacter sphaeroides and Crystallography. The concepts of his Photosynthetic reaction centre study are interwoven with issues in Photosynthetic bacteria, Electron transport chain and Stereochemistry. His work in the fields of Proton-coupled electron transfer overlaps with other areas such as Reaction rate constant.
His Photochemistry study incorporates themes from Photosynthesis, Bacteriochlorophyll and Electron paramagnetic resonance, Semiquinone. Melvin Y. Okamura has included themes like Hydrogen bond, Redox, Mutant and Quinone in his Rhodobacter sphaeroides study. The Crystallography study combines topics in areas such as Electrostatics, Pheophytin and Atomic physics.
Melvin Y. Okamura mostly deals with Photosynthetic reaction centre, Photochemistry, Electron transfer, Rhodobacter sphaeroides and Crystallography. His Photosynthetic reaction centre research includes themes of Photosynthetic bacteria and Stereochemistry. His research in Photochemistry intersects with topics in Nanotechnology, Electron transport chain, Hydrogen bond and Quinone.
His study in Electron transfer is interdisciplinary in nature, drawing from both Electron paramagnetic resonance, Protonation and Analytical chemistry. His Rhodobacter sphaeroides research incorporates elements of Ground state and Bacteriochlorophyll. His work in Crystallography addresses subjects such as Electron acceptor, which are connected to disciplines such as Atomic physics.
His primary scientific interests are in Photochemistry, Electron transfer, Rhodobacter sphaeroides, Photosynthetic reaction centre and Hydrogen bond. His research integrates issues of Protein structure, Electron transport chain and Semiquinone, Quinone in his study of Photochemistry. His Protein structure study combines topics from a wide range of disciplines, such as Stereochemistry and Binding constant.
His Quinone research is multidisciplinary, incorporating perspectives in Membrane protein complex, Dimer and Solvent molecule. Melvin Y. Okamura has researched Rhodobacter sphaeroides in several fields, including Quinone binding and Bacteriochlorophyll. His research investigates the connection between Bacteriochlorophyll and topics such as Quantum yield that intersect with problems in Photosynthetic bacteria.
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Structure and function of bacterial photosynthetic reaction centres
G. Feher;J. P. Allen;M. Y. Okamura;D. C. Rees.
Primary acceptor in bacterial photosynthesis: obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas spheroides.
M Y Okamura;R A Isaacson;G Feher.
Proceedings of the National Academy of Sciences of the United States of America (1975)
Proton and electron transfer in bacterial reaction centers.
M.Y Okamura;M.L Paddock;M.S Graige;G Feher.
Biochimica et Biophysica Acta (2000)
Protonation of interacting residues in a protein by a Monte Carlo method: application to lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides.
P Beroza;D R Fredkin;M Y Okamura;G Feher.
Proceedings of the National Academy of Sciences of the United States of America (1991)
Pathway of proton transfer in bacterial reaction centers: replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover.
M L Paddock;S H Rongey;G Feher;M Y Okamura.
Proceedings of the National Academy of Sciences of the United States of America (1989)
Iron-depleted reaction centers from Rhodopseudomonas sphaeroides R-26.1: characterization and reconstitution with Fe2+, Mn2+, Co2+, Ni2+, Cu2+, and Zn2+.
R. J. Debus;G. Feher;M. Y. Okamura.
Electron transfer in reaction centers of Rhodopseudomonas sphaeroides. I. Determination of the charge recombination pathway of D+QAQ(-)B and free energy and kinetic relations between Q(-)AQB and QAQ(-)B.
D. Kleinfeld;M.Y. Okamura;G. Feher.
Biochimica et Biophysica Acta (1984)
Spectroscopic and kinetic properties of the transient intermediate acceptor in reaction centers of Rhodopseudomonas sphaeroides.
M.Y. Okamura;R.A. Isaacson;G. Feher.
Biochimica et Biophysica Acta (1979)
Identification of an electron acceptor in reaction centers of Rhodopseudomonas spheroides by EPR spectroscopy
G. Feher;M.Y. Okamura;J.D. McElroy.
Biochimica et Biophysica Acta (1972)
Mechanism of Proton-Coupled Electron Transfer for Quinone (QB) Reduction in Reaction Centers of Rb. Sphaeroides
M. S. Graige;M. L. Paddock;J. M. Bruce;G. Feher.
Journal of the American Chemical Society (1996)
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