Literature DB >> 10348620

Heme-mediated oxygen activation in biology: cytochrome c oxidase and nitric oxide synthase.

T L Poulos1, H Li, C S Raman.   

Abstract

Major advances have been made in our understanding of cytochrome c oxidase owing to continued crystallographic work on important intermediates. This, together with a wealth of data derived from selective mutations and sophisticated spectroscopic probes, has provided significant new insights into oxidase dioxygen chemistry and proton pumping activities. Recent advances have also been made for nitric oxide synthase, owing to the crystal structure determination of the heme domain for two of three nitric oxide synthase isoforms.

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Year:  1999        PMID: 10348620     DOI: 10.1016/s1367-5931(99)80024-6

Source DB:  PubMed          Journal:  Curr Opin Chem Biol        ISSN: 1367-5931            Impact factor:   8.822


  9 in total

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8.  The role of copper and protons in heme-copper oxidases: kinetic study of an engineered heme-copper center in myoglobin.

Authors:  Jeffrey A Sigman; Hyeon K Kim; Xuan Zhao; James R Carey; Yi Lu
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Review 9.  One heme, diverse functions: using biosynthetic myoglobin models to gain insights into heme-copper oxidases and nitric oxide reductases.

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  9 in total

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