Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands.
    

concept

Molecular model of cytochrome oxidase, ribbon

The history of cell respiration and cytochrome / Prepared for publication by Joan Keilin.

Biological electron transfer chains : genetics, composition, and mode of operation / edited by G.W. Canters and E. Vijgenboom.

Cytochrome synthesis, growth and cell division in a strain of ustilago sphaerogena / by Edward Spoerl, Norma Puckett and Alvin Sarachek.

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Molecular model of cytochrome oxidase, ribbon

The history of cell respiration and cytochrome / Prepared for publication by Joan Keilin.

Molecular model of cytochrome oxidase, ribbon

Biological electron transfer chains : genetics, composition, and mode of operation / edited by G.W. Canters and E. Vijgenboom.

Cytochrome synthesis, growth and cell division in a strain of ustilago sphaerogena / by Edward Spoerl, Norma Puckett and Alvin Sarachek.