A textbook of inorganic chemistry vol.VII part III Chromium by Newton [Ed] Friend

By Newton [Ed] Friend

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A crystallographic study with M314I PHM revealed a number of interesting results. Predictably, structural alignment between oxidized M314I PHM and the published structure of oxidized PHM showed significant changes close to the CuM site. Displacement of the mutated residue, Ile314, from CuM resulted in disorder of the flanking loop (299–313) and caused loop 212–218 ˚ away from CuM. Unexpectedly, replacement of the Met314 ligand to move as far as 5 A does not prohibit copper binding at the CuM site.

And Penicillium olsonii,11 the FDO protein of Streptomyces sp. 32,33 First, we give a brief overview of the studies on the enzymatic reaction and the structure of the enzymatic active site from A. japonicus. A more detailed insight will be presented into the mechanistic details of the oxygenation reactions including the mode of the O2 activation carried out with model substrates. We provide a thorough understanding of the influence of metal and ligand moieties, as well as those of the substrate coordination modes on the reaction mechanism.

E. The biosynthesis of neuropeptides: Peptide a-amidation Annu. Rev. Neurosci. 1992, 15, 57–85. 16. Klinman, J. ; Edmondson, D. E. Evidence for two copper atoms/subunit in dopamine beta-monooxygenase catalysis J. Biol. Chem. 1984, 259, 3399–3402. 17. ; Ljones, T. Direct spectrophotometric detection of ascorbate free radical formed by dopamine b-monooxygenase and by ascorbate oxidase Biochim. Biophys. Acta 1980, 630, 30–35. 18. Diliberto, E. ; Allen, P. L. Mechanism of dopamine-b-hydroxylation. Semidehydroascorbate as the enzymic oxidation product of ascorbate J.

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