2000 - Fellow of the American Association for the Advancement of Science (AAAS)
His primary areas of investigation include Photochemistry, Cytochrome, Stereochemistry, Electron transfer and Reaction rate constant. Michael A. Cusanovich studies Chromophore which is a part of Photochemistry. His work deals with themes such as Flavoprotein and Heme, which intersect with Cytochrome.
His biological study deals with issues like Flavin group, which deal with fields such as Mutant. The various areas that he examines in his Stereochemistry study include Amino acid, Crystallography, Respiratory chain and Succinate dehydrogenase, Fumarate reductase. His Electron transfer research focuses on Redox and how it relates to Ferredoxin.
His main research concerns Cytochrome, Photochemistry, Stereochemistry, Heme and Biochemistry. His Cytochrome research includes elements of Photosynthetic reaction centre, Crystallography, Cytochrome b, Rhodobacter and Hemeprotein. His Electron transfer and Chromophore study, which is part of a larger body of work in Photochemistry, is frequently linked to Reaction rate constant and Ionic strength, bridging the gap between disciplines.
His Electron transfer study combines topics from a wide range of disciplines, such as Redox, Electron transport chain, Ferredoxin and Rhodospirillum rubrum. His Stereochemistry study integrates concerns from other disciplines, such as Protein structure and Crystal structure. His work on Heme binding as part of general Heme research is frequently linked to Ligand, bridging the gap between disciplines.
His primary areas of study are Photochemistry, Stereochemistry, Cytochrome, Chromophore and Biochemistry. Michael A. Cusanovich merges many fields, such as Photochemistry and Reaction rate constant, in his writings. His Stereochemistry study incorporates themes from Crystallography, Crystal structure, Shewanella oneidensis, Heme and Protein structure.
His Heme study combines topics in areas such as Redox and Electron transfer. His studies in Cytochrome integrate themes in fields like Photosynthetic reaction centre, Cytochrome b6f complex, Cytochrome b and Rhodobacter. His work on Purple bacteria, Rhodobacter sphaeroides, Photosynthetic bacteria and Escherichia coli as part of general Biochemistry research is frequently linked to PAS domain, thereby connecting diverse disciplines of science.
The scientist’s investigation covers issues in Biochemistry, Cytochrome, Photochemistry, Shewanella oneidensis and PAS domain. His research in Biochemistry intersects with topics in Shewanella putrefaciens and Desulfovibrio. His studies examine the connections between Cytochrome and genetics, as well as such issues in Coenzyme Q – cytochrome c reductase, with regards to Cytochrome b6f complex, Cytochrome c peroxidase and Molecular biology.
His research in Photochemistry is mostly concerned with Chromophore. His Shewanella oneidensis research is multidisciplinary, incorporating perspectives in Heme binding, Heme, Electron transfer, Redox and Fumarate reductase. His work in Heme covers topics such as Oxidoreductase which are related to areas like Stereochemistry.
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Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin
T. E. Meyer;E. Yakali;M. A. Cusanovich;G. Tollin.
The environment of Fe4S4 clusters in ferredoxins and high-potential iron proteins. New information from x-ray crystallography and resonance Raman spectroscopy
Gabriele Backes;Yoshiki Mino;Thomas M. Loehr;Terrence E. Meyer.
Journal of the American Chemical Society (1991)
Photoactive yellow protein from the purple phototrophic bacterium, Ectothiorhodospira halophila. Quantum yield of photobleaching and effects of temperature, alcohols, glycerol, and sucrose on kinetics of photobleaching and recovery.
T.E. Meyer;G. Tollin;J.H. Hazzard;M.A. Cusanovich.
Biophysical Journal (1989)
Active Site Mutants Implicate Key Residues for Control of Color and Light Cycle Kinetics of Photoactive Yellow Protein
Ulrich K. Genick;Savitha Devanathan;Terry E. Meyer;Ilona L. Canestrelli.
Identification of 42 possible cytochrome C genes in the Shewanella oneidensis genome and characterization of six soluble cytochromes.
Terry E. Meyer;Alexandre I. Tsapin;Isabel Vandenberghe;Lina De Smet.
Omics A Journal of Integrative Biology (2004)
Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein
J.A. Kyndt;T.E. Meyer;M.A. Cusanovich;J.J. Van Beeumen.
FEBS Letters (2002)
Photoactive Yellow Protein: A Prototypic PAS Domain Sensory Protein and Development of a Common Signaling Mechanism†
Michael A. Cusanovich;Terry E. Meyer.
New photocycle intermediates in the photoactive yellow protein from Ectothiorhodospira halophila: picosecond transient absorption spectroscopy.
L. Ujj;S. Devanathan;T.E. Meyer;M.A. Cusanovich.
Biophysical Journal (1998)
The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium
Zhi-Wei Chen;Monjoo Koh;G. Van Driessche;J. J. Van Beeumen.
Tryptophan-191----phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation.
Mauro Jm;Fishel La;Hazzard Jt;Meyer Te.
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