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• W2024260356 abstract "The six-electron reductions of sulfite to sulfide and nitrite to ammonia, fundamental to early and contemporary life, are catalyzed by diverse sulfite and nitrite reductases that share an unusual prosthetic assembly in their active centers, namely siroheme covalently linked to an Fe4S4 cluster. The recently determined crystallographic structure of the sulfite reductase hemoprotein from Escherichia coli complements extensive biochemical and spectroscopic studies in revealing structural features that are key for the catalytic mechanisms and in suggesting a common symmetric structural unit for this diverse family of enzymes." @default.
• W2024260356 created "2016-06-24" @default.
• W2024260356 creator A5020111798 @default.
• W2024260356 creator A5071526287 @default.
• W2024260356 date "1996-12-01" @default.
• W2024260356 modified "2023-10-17" @default.
• W2024260356 title "The relationship between structure and function for the sulfite reductases" @default.
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• W2024260356 doi "https://doi.org/10.1016/s0959-440x(96)80003-0" @default.
• W2024260356 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8994874" @default.
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