D-Index & Metrics Best Publications

D-Index & Metrics D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines.

Discipline name D-index D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines. Citations Publications World Ranking National Ranking
Chemistry D-index 59 Citations 9,980 250 World Ranking 6970 National Ranking 2161

Research.com Recognitions

Awards & Achievements

2000 - Fellow of the American Association for the Advancement of Science (AAAS)

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Amino acid
  • Gene

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 most cited work include:

  • Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin (224 citations)
  • The environment of Fe4S4 clusters in ferredoxins and high-potential iron proteins. New information from x-ray crystallography and resonance Raman spectroscopy (194 citations)
  • Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein (148 citations)

What are the main themes of his work throughout his whole career to date?

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.

He most often published in these fields:

  • Cytochrome (43.87%)
  • Photochemistry (34.78%)
  • Stereochemistry (30.43%)

What were the highlights of his more recent work (between 2000-2013)?

  • Photochemistry (34.78%)
  • Stereochemistry (30.43%)
  • Cytochrome (43.87%)

In recent papers he was focusing on the following fields of study:

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.

Between 2000 and 2013, his most popular works were:

  • Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein (148 citations)
  • Identification of 42 possible cytochrome C genes in the Shewanella oneidensis genome and characterization of six soluble cytochromes. (144 citations)
  • Photoactive Yellow Protein: A Prototypic PAS Domain Sensory Protein and Development of a Common Signaling Mechanism† (123 citations)

In his most recent research, the most cited papers focused on:

  • Enzyme
  • Amino acid
  • Gene

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.

This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.

Best Publications

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.
Biochemistry (1987)

375 Citations

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)

352 Citations

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)

243 Citations

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.
Biochemistry (1997)

217 Citations

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)

216 Citations

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)

213 Citations

Photoactive Yellow Protein: A Prototypic PAS Domain Sensory Protein and Development of a Common Signaling Mechanism†

Michael A. Cusanovich;Terry E. Meyer.
Biochemistry (2003)

204 Citations

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)

200 Citations

The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium

Zhi-Wei Chen;Monjoo Koh;G. Van Driessche;J. J. Van Beeumen.
Science (1994)

189 Citations

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.
Biochemistry (1988)

187 Citations

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