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• W1973148373 abstract "Reaction pathways in the enzymatic formation and cleavage of the N−N and N−O bonds, respectively, are difficult to verify without the structure of the intermediates, but we now have such information on the heme a32+-NO species formed in the reaction of ba3-oxidase with NO from resonance Raman spectroscopy. We have identified the His-heme a32+-NO/CuB1+ species by its characteristic Fe−NO and N−O stretching frequencies at 539 and 1620 cm-1, respectively. The Fe−NO and N−O frequencies in ba3-oxidase are 21 and 7 cm-1 lower and higher, respectively, than those observed in Mb−NO. From these results and earlier Raman and FTIR measurements, we demonstrate that the protein environment of the proximal His384 that is part of the Q-proton pathway controls the strength of the Fe−His384 bond upon ligand (CO vs NO) binding. We also show by time-resolved FTIR spectroscopy that CuB1+ has a much lower affinity for NO than for CO. We suggest that the reduction of NO to N2O by ba3-oxidase proceeds by the fast binding of the first NO molecule to heme a3 with high-affinity, and the second NO molecule binds to CuB with low-affinity, producing the temporal co-presence of two NO molecules in the heme-copper center. The low-affinity of CuB for NO binding also explains the NO reductase activity of the ba3-oxidase as opposed to other heme-copper oxidases. With the identification of the His-heme a32+-NO/CuB1+ species, the structure of the binuclear heme a3-CuB1+ center in the initial step of the NO reduction mechanism is known." @default.
• W1973148373 created "2016-06-24" @default.
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• W1973148373 date "2005-10-04" @default.
• W1973148373 modified "2023-10-12" @default.
• W1973148373 title "Detection of the His-Heme Fe²⁺−NO Species in the Reduction of NO to N₂O by <i>b</i><i>a</i>₃-Oxidase from <i>Thermus </i><i>t</i><i>hermophilus</i>" @default.
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• W1973148373 doi "https://doi.org/10.1021/ja0539490" @default.
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