Skip to search formSkip to main contentSkip to account menu

Cytochromes

Known as: Cytochrome, Cytochromes [Chemical/Ingredient] 
Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation… 
National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
1993
1993
The visible absorption and Soret-excited resonance Raman spectra of ferrous microperoxidase-8 [MP8(II)], an octapeptide… 
Highly Cited
1984
Highly Cited
1984
We have measured the ionic strength dependence of the rate constants for electron transfer from the semiquinone of Clostridium… 
Highly Cited
1984
Highly Cited
1984
The method of continuous saturation has been used to measure the electron spin relaxation parameter T1T2 at temperatures between… 
1984
1984
Chemically modified spinach plastocyanin, in which negatively charged carboxyl residues are replaced with positively charged… 
Review
1982
Review
1982
A review of the literature concerning the structure and electron-transfer function of cytochrome c is presented. Emphasis is… 
1980
1980
Cytochrome c-552 from Chromatium vinosum is an unusual heme protein in that it contains two hemes and one flavin per molecule. To… 
1979
1979
The kinetics of the oxidation-reduction reactions between horse heart cytochrome c, Euglena gracilis cytochrome c552, and ions… 
1978
1978
Resonance Raman spectra have been measured for cytochromes P-450 purified from liver microsomes of phenobarbital-treated rabbits… 
1975
1975
Magnetic circular dichroism (MCD) spectra have been measured for cytochrome P-450 (P-450) purified from phenobarbital-induced… 
1963
1963
The cytochrome oxidase activity was estimated in homogenates of the whole body and in nine body organs of cold- and warm…