Skip to search formSkip to main contentSkip to account menu

Cytochromes c2

Known as: Cytochrome c2, Ferrocytochrome c2, Cytochrome C 2 
Type C cytochromes that are small (12-14 kD) single-heme proteins. They function as mobile electron carriers between membrane-bound enzymes in… 
National Institutes of Health

Related topics

Related topics

7 relations
In BloodProcess of secretionantagonists & inhibitorsaspects of radiation effects

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2004
2004
Shotgun proteomic analysis of a chromatophore-enriched preparation from the purple phototrophic bacterium Rhodopseudomonas palustris
A proteomics approach was evaluated for analysis of photosyntheis-related proteins that are characteristic of chromatophores… 
2003
2003
Theoretical understanding of the interprotein electron transfer between cytochrome c2 and the photosynthetic reaction center
Interprotein electron transfer (ET) reactions play a central role in the early steps in bioenergetic processes such as… 
1997
1997
Structure and function of cytochrome c2 in electron transfer complexes with the photosynthetic reaction center of Rhodobacter sphaeroides: optical linear dichroism and EPR.
The photosynthetic reaction center (RC) and its secondary electron donor the water-soluble cytochrome (cyt) c2 from the purple… 
Highly Cited
1990
Highly Cited
1990
Mutants of ubiquinol-cytochrome c2 oxidoreductase resistant to Qo site inhibitors: consequences for ubiquinone and ubiquinol affinity and catalysis.
Seven single-site mutants in six residues of the cyt b polypeptide of Rhodobacter capsulatus selected for resistance to the Qo… 
1987
1987
Reaction of cytochromes c and c2 with the Rhodobacter sphaeroides reaction center involves the heme crevice domain.
In order to define the interaction domain on Rhodobacter sphaeroides cytochrome c2 for the photosynthetic reaction center… 
Highly Cited
1986
Highly Cited
1986
Discrete catalytic sites for quinone in the ubiquinol-cytochrome c2 oxidoreductase of Rhodopseudomonas capsulata. Evidence from a mutant defective in ubiquinol oxidation.
A non-photosynthetic mutant (Ps-) of Rhodopseudomonas capsulata, designated R126, was analyzed for a defect in the cyclic… 
1986
1986
Electron-transfer reactions between flavodoxin semiquinone and c-type cytochromes: comparisons between various flavodoxins.
As an extension of previous work from this laboratory using Clostridium pasteurianum flavodoxin [Tollin, G., Cheddar, G., Watkins… 
Highly Cited
1984
Highly Cited
1984
Electron-transfer reactions of photoreduced flavin analogues with c-type cytochromes: quantitation of steric and electrostatic factors.
We have found correlations between rate constants and the difference in redox potential of the reactants for electron-transfer… 
1979
1979
Proton nuclear magnetic resonance studies of Rhodospirillum rubrum cytochrome.
Rhodospirillum rubrum cytochrome c2 was studied by proton nuclear magnetic resonance at 220 MHz. Assignments were made to the… 
Highly Cited
1978
Highly Cited
1978
Second order kinetics of the reduction of cytochrome c2 by the ubiquinone cytochrome b-c2 oxidoreductase of Rhodopseudomonas sphaeroides.
The direct reductant of ferricytochrome c2 in the ubiquinone cytochrome b-c2 oxidoreductase of Rhodopseudomonas sphaeroides is a…