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• W1985137922 abstract "Nostoc sp. (Ns) H-NOX is a heme protein found in symbiotic cyanobacteria, which has ∼35% sequence identity and high structural homology to the β subunit of soluble guanylyl cyclase (sGC), suggesting a NO sensing function. However, UV−vis, EPR, NIR MCD, and ligand binding experiments with ferrous and ferric Ns H-NOX indicate significant functional differences between Ns H-NOX and sGC. (1) After NO binding to sGC, the proximal histidine dissociates from the heme iron, causing a conformational change that triggers activation of sGC. In contrast, formation of pentacoordinate (5c) NO heme occurs to only a limited extent in Ns H-NOX, even at >1 mM NO. (2) Unlike sGC, two different hexacoordinate (6c) NO complexes are formed in Ns H-NOX with initial and final absorbance peaks at 418 and 414 nm, and the conversion rate is linearly dependent on [NO], indicating that a second NO binds transiently to catalyze formation of the 414 nm species. (3) sGC is insensitive to oxygen, and ferric sGC prepared by ferricyanide oxidation has a 5c high-spin heme complex. In contrast, Ns H-NOX autoxidizes in 24 h if exposed to air and forms a 6c ferric heme complex, indicating a major conformational change after oxidation and coordination by a second histidine side chain. Such a large conformational transition suggests that Ns H-NOX could function as either a redox or a NO sensor in the cyanobacterium." @default.
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• W1985137922 date "2010-07-14" @default.
• W1985137922 modified "2023-09-30" @default.
• W1985137922 title "Is <i>Nostoc</i> H-NOX a NO Sensor or Redox Switch?" @default.
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• W1985137922 doi "https://doi.org/10.1021/bi1002234" @default.
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