WordNet

an enzyme that catalyzes oxidation-reduction
within the molecule; occurring by a reaction between different parts of the same molecule

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Ghezzi P.SourceBrighton & Sussex Medical School, Trafford Centre, Falmer, BN19RY, UK. Electronic address: p.ghezzi@bsms.ac.uk.
Biochimica et biophysica acta.Biochim Biophys Acta.2013 May;1830(5):3165-72. doi: 10.1016/j.bbagen.2013.02.009. Epub 2013 Feb 15.
BACKGROUND: It is now recognized that protein cysteines exist not only as free thiols or intramolecular disulfides, that help maintain the 3D structure of proteins, but can also undergo different types of oxidation, one of which is glutathionylation, or the formation of mixed disulfides with glutath
PMID 23416063

Hirst J.SourceMedical Research Council Mitochondrial Biology Unit, Cambridge, CB2 OXY, United Kingdom; email: jh@mrc-mbu.cam.ac.uk.
Annual review of biochemistry.Annu Rev Biochem.2013 Mar 18. [Epub ahead of print]
Complex I (NADH:ubiquinone oxidoreductase) is crucial for respiration in many aerobic organisms. In mitochondria, it oxidizes NADH from the tricarboxylic acid cycle and β-oxidation, reduces ubiquinone, and transports protons across the inner membrane, contributing to the proton-motive force. It is
PMID 23527692

Steady-state catalytic wave-shapes for 2-electron reversible electrocatalysts and enzymes.

Fourmond V, Baffert C, Sybirna K, Lautier T, Abou Hamdan A, Dementin S, Soucaille P, Meynial-Salles I, Bottin H, Léger C.SourceCNRS, Aix-Marseille Univ, BIP UMR 7281, IMM FR 3479, 31 chemin J. Aiguier, 13402 Marseille Cedex 20, France.
Journal of the American Chemical Society.J Am Chem Soc.2013 Mar 13;135(10):3926-38. doi: 10.1021/ja311607s. Epub 2013 Mar 1.
Using direct electrochemistry to learn about the mechanism of electrocatalysts and redox enzymes requires that kinetic models be developed. Here we thoroughly discuss the interpretation of electrochemical signals obtained with adsorbed enzymes and molecular catalysts that can reversibly convert thei
PMID 23362993

Prebiotic evolution of oxidoreductases: (Fe(III)(CN)5(L))n- complexes as models.

Kamaluddin,Mala Nath,Sushama W. Deopujari
Bulletin of the Chemical Society of Japan 62(10), 3291-3297, 1989
… partially replaced by biomolecules, has been assumed to be interesting from point of view of chemical evolution of oxidoreductase enzymes. … binds to <SUP>−</SUP>OH through weak intramolecular hydrogen bonding, formation of peroxo complexes has been proposed to be an active intermediate responsible for accelerating the reaction. …
NAID 130001980741

Purification and characterization of the assimilatory NADPH-nitrate reductase of Aspergillus nidulans.

MINAGAWA Nobuko,YOSHIMOTO Akio
The Journal of Biochemistry 91(3), 761-774, 1982
… NADPH-nitrate reductase [NADPH : nitrate oxidoreductase, EC 1. … It was concluded that a b-type cytochrome ("cytochrome b-557") is present in the enzyme and is involved in the intramolecular electron transport from NADPH to nitrate. …
NAID 130003542124

The Kinetic Behavior of the FMN and Protoheme Moieties of Yeast L(+)-Lactate Dehydrogenase (Cytochrome b2)

SUZUKI HARUO,OGURA YASUYUKI
The Journal of Biochemistry 67(2), 277-289, 1970
… 3, L-lactate: ferricytochrome c oxidoreductase], were estimated spectrophotometrically by the "stopped flow method." The rates of reduction of these prosthetic groups were measured also with the "continuous flow method" by mixing the oxidized enzyme with a solution of the substrate under anaerobic conditions. …
NAID 130003418715