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Flavin adenine dinucleotide, reduced

This thiol-disulfide interconversion is a key part of numerous biological processes. WeTJ see in Chapter 26, for instance, that disulfide formation is involved in defining the structure and three-dimensional conformations of proteins, where disulfide "bridges" often form cross-links between q steine amino acid units in the protein chains. Disulfide formation is also involved in the process by which cells protect themselves from oxidative degradation. A cellular component called glutathione removes potentially harmful oxidants and is itself oxidized to glutathione disulfide in the process. Reduction back to the thiol requires the coenzyme flavin adenine dinucleotide (reduced), abbreviated FADH2. [Pg.668]

EADH2 flavin adenine dinucleotide, reduced form... [Pg.420]

Fig. 1. Energy metabolism in the normal myocardium (ATP adenosine-5 -triphosphate, ADP adenosine-5 -diphosphate, P phosphate, PDH pyruvate dehydrogenase complex, acetyl-CoA acetyl-coenzyme A, NADH and NAD" nicotinamide adenine dinucleotide (reduced and oxidized), FADH2 and FAD flavin adenine dinucleotide (reduced and oxidized). Fig. 1. Energy metabolism in the normal myocardium (ATP adenosine-5 -triphosphate, ADP adenosine-5 -diphosphate, P phosphate, PDH pyruvate dehydrogenase complex, acetyl-CoA acetyl-coenzyme A, NADH and NAD" nicotinamide adenine dinucleotide (reduced and oxidized), FADH2 and FAD flavin adenine dinucleotide (reduced and oxidized).
Fig. 1.12. Schematb drawing of the glucose oxidase molecule, showing the electron-transfer distances involved in the various steps of moving an electron from its two flavin adenine dinucleotide/reduced flavin adenine dinucleotide (FAD/FADHg) centers to a metal electrode. Left The enzyme before modification. Right The modified enzyme, after chemical attachment of an array of electron transfer relays ( R ). (Reprinted from Y. Degani and A. Heller, J. Phys. Chem. 91 1286, 1987.)... Fig. 1.12. Schematb drawing of the glucose oxidase molecule, showing the electron-transfer distances involved in the various steps of moving an electron from its two flavin adenine dinucleotide/reduced flavin adenine dinucleotide (FAD/FADHg) centers to a metal electrode. Left The enzyme before modification. Right The modified enzyme, after chemical attachment of an array of electron transfer relays ( R ). (Reprinted from Y. Degani and A. Heller, J. Phys. Chem. 91 1286, 1987.)...
FAD flavin adenine dinucleotide (oxidized form) FADH2 flavin adenine dinucleotide (reduced form) fMet formylmethionine FMN flavin mononucleotide (oxidized form) FMNH2 flavin mononucleotide (reduced form)... [Pg.1512]

BPG Bisphosphoglycerate FADH2 Flavin adenine dinucleotide (reduced)... [Pg.963]

Flavin adenine dinucleotide reduced form FADH2... [Pg.169]

Coenzymes and energy suppliers FADI(H) flavin adenine dinucleotide/(reduced) NADI(H) nicotinamide adenine dinucleotide/(reduced) GTP guanosine triphosphate ATP adenosine triphosphate UTP uridine triphosphate GDP guanosine diphosphate ADP adenosine diphosphate AMP adenosine monophosphate CoA coenzyme A. Based on Ching, 1972 [5]... [Pg.203]

FIGURE 2 Some important reactions in metabolism. Shown are the phosphorylation of ADP to ATP, NAD+, NADH, FAD, FADH2 acetate, CoA, and acetyl CoA. For clarity, just the parts of the larger molecules that undergo reaction are shown. NAD+, nicotinamide adenine dinucleotide NADH, nicotinamide adenine dinucleotide (reduced form) FAD, flavin adenine dinucleotide FADH2, flavin adenine dinucleotide (reduced form) CoA, coenzyme A AMP, adenosine monophosphate. [Pg.5]

Ethylene diamine tetraacetic acid Flavin-adenine dinucleotide Flavin-adenine dinucleotide, reduced form Flavin mononucleotide Follicle-stimulating hormone Glucose dehydrogenase a-Glycerophosphate (glycerol 1-phosphate)... [Pg.398]


See other pages where Flavin adenine dinucleotide, reduced is mentioned: [Pg.63]    [Pg.16]    [Pg.447]    [Pg.447]    [Pg.4]    [Pg.600]    [Pg.668]    [Pg.1116]    [Pg.358]    [Pg.358]    [Pg.453]    [Pg.1191]    [Pg.386]    [Pg.1221]   


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