Cytochrome b -245 is a flavocytochrome containing FAD and the NADPH-binding site of the microbicidal oxidase of phagocytes

• Published in: Biochemical journal Vol. 284; no. 3; pp. 781 - 788
• Main Authors: Segal, A W, West, I, Wientjes, F, Nugent, J H A, Chavan, A J, Haley, B, Garcia, R C, Rosen, H, Scrace, G
• Format: Journal Article
• Language: English
• Published: Colchester Portland Press 15.06.1992
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Binding Sites; Biological and medical sciences; Cell Line; Cell Membrane - metabolism; Chromatography, Affinity; Chromatography, Ion Exchange; Cytochrome b Group - chemistry; Cytochrome b Group - isolation & purification; Cytochrome b Group - metabolism; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide - analysis; Flavin-Adenine Dinucleotide - metabolism; Fundamental and applied biological sciences. Psychology; Heme - analysis; Heme - metabolism; Hemoproteins; Humans; Macromolecular Substances; Metalloproteins; Models, Structural; Molecular Sequence Data; Molecular Weight; NADH, NADPH Oxidoreductases - blood; NADP - metabolism; NADPH Oxidases; Neutrophils - enzymology; Oxidation-Reduction; Phagocytosis; Protein Conformation; Proteins; Rats; Sequence Homology, Nucleic Acid; Superoxides - metabolism; Human; NADPH; Cytochrome b; Enzyme; Plasma membrane; Molecular association; FAD; Neutrophil

The NADPH oxidase of phagocytic cells is important for the efficient killing and digestion of ingested microbes. A very unusual low-potential cytochrome b (b-245) is the only redox molecule to have been identified in this system. The FAD-containing flavoprotein that binds NADPH and transfers electro...