Biochemistry by J D Dunitz PDF

By J D Dunitz

ISBN-10: 354009816X

ISBN-13: 9783540098164

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1 Prolyl Hydroxylase . . . . . . . . . . . . . . . . . . . . . 2 p-Hydroxyphenyipytuvate Hydroxyiase . . . . . . . . . . . . . . . 63 63 66 4 Lipoxygenase . . . . . . . . . . . . . . . . . . . . . . 67 5 Summary . . . . . . . . . . . . . . . . . . . . . . . 69 6 References . . . . . . . . . . . . . . . . . . . . . . . 70 Recent progress in understanding the structure and mechanism o f nonheme iron dioxygenases is discussed; three classes o f dioxygenases are reviewed - the intradiol cleaving catechol dioxygenases, the ~ketoglutarate dioxygenases, and lipoxygenase.

67 5 Summary . . . . . . . . . . . . . . . . . . . . . . . 69 6 References . . . . . . . . . . . . . . . . . . . . . . . 70 Recent progress in understanding the structure and mechanism o f nonheme iron dioxygenases is discussed; three classes o f dioxygenases are reviewed - the intradiol cleaving catechol dioxygenases, the ~ketoglutarate dioxygenases, and lipoxygenase. In all three classes o f enzymes, iron is essential for the catalysis o f dioxygen fixation reactions, though the mechanisms by which these reactions are r~alized appeax to be quite distinct from each other.

New peaks assigned to the inhJbitors are also observed, indicating that the phenolates bind to the active site iron. We have explored the resonance Raman spectrum of protocatechuate 3,4-dioxygenase with m-hydroxybenzoate. The visible spectrum of the complex is slightly blueshifted from the native enzyme (456 -~ 445 rim). 1 um excitation) exhibits no new vibrations suggestingthat, in contrast to the p-hydroxybenzoates, the m-OH group does not coordinate to the iron. 49 L. Que, Jr. 2 x 4 2 4 nm native protocotechuate ~ 3,4 -dioxygenase \ ~ / ' X m a x 456nm - I-o - chlorophenol ..

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Biochemistry by J D Dunitz


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