Titlebook: Iron and Copper Proteins; Kerry T. Yasunodu,Howard F. Mower,Osamu Hayaishi Book 1976 The Editor(s) (if applicable) and The Author(s), unde

横条

Evidence for Participation of NADH-Dependent Reductase in the Reaction of Benzoate 1,2-Dioxygenase (ation of two hydroxyl groups into benzoate, resulting in the formation of l,2-dihydro-l,2-dihydroxybenzoate (DHB). Both oxygen atoms of the two hydroxyl groups introduced into the substrate are derived from the molecular oxygen (1,2).

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Subunit Structure of Nonheme Iron-Containing Dioxygenasesin all types of living organisms and shown to perform a variety of functions. Among these, cleavage of the aromatic ring is one function that appears to depend largely, perhaps entirely, upon this type of enzyme. Cofactors involved in these enzymes are nonheme iron, heme or copper (1). The indole ri

作茧自缚

Iron-Sulfur Proteins, the Most Numerous and Most Diversified Components of the Mitochondrial Electrowithin the past few years of three volumes of a treatise exclusively devoted to these compounds (1). The great number and variety of recently discovered plant, bacterial and mammalian Fe-S proteins and of the reactions catalyzed by them, exemplify this progress. This presentation will focus on the l

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FLACK

Biochemical and EPR Probes for Structure-Function Studies of Iron Sulfur Centers of Succinate Dehydrelectron transport. Perhaps because it is tenaciously attached to the membrane and “uniquely” reacts with electron acceptors, reports on the serious attempts of its solubilization did not appear until 1955. It is true that Tsou in 1950 definitively established the non-identity of succinate dehydroge

Sigmoidoscopy

Heme , and Copper Environments in Cytochrome Oxidaseration of yeast suspensions by illumination, and predicted the heme-like nature of the active site of this enzyme (Warburg and Negelein, 1928). Ten years later, from spectral examinations of the effect of several respiratory inhibitors on the heart muscle preparation, Keilin and Hartree postulated t

expound

Heme Interactions in , Cytochrome Oxidasedonate electrons either to molecular oxygen or to nitrite although it appears that . it is intended to react with nitrite rather than 02 since the enzyme is only synthesized when the organism is grown anaerobically in the presence of nitrate or nitrite. However, since . cytochrome oxidase can cataly

scoliosis

Equilibrium States and Dynamic Reactions of Iron in the Camphor Monoxygenase Systemnergy. This chapter, in dealing with molecular enzymology, focuses on the latter commodity and deals with the . class of enzymes which, together with the other catalytic and metabolic systems, are ubiquitous in nature and required by many living organisms for existence.

arabesque

Current Status of the Sequence Studies of the , Camphor Hydroxylase System hydroxylase fraction known as soluble cytochrome P-450 (1). This mixed function oxidase catalyzes the hydroxylation of methylene carbon 5 of camphor with reduced diphosphopyridine nucleotide as the primary electron donor and with molecular oxygen as the acceptor. The physicochemical and kinetic pro