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• W3019972607 abstract "Transient absorption, resonance Raman, and vibrational coherence spectroscopies are used to investigate the mechanisms of NO and O₂ binding to WT Tt H-NOX and its P115A mutant. Vibrational coherence spectra of the oxy complexes provide clear evidence for the enhancement of an iron–histidine mode near 217 cm–¹ following photoexcitation, which indicates that O₂ can be dissociated in these proteins. However, the quantum yield of O₂ photolysis is low, particularly in the wild type (≲3%). Geminate recombination of O₂ and NO in both of these proteins is very fast (∼1.4 × 10¹¹ s–¹) and highly efficient. We show that the distal heme pocket of the H-NOX system forms an efficient trap that limits the O₂ off-rate and determines the overall affinity. The distal pocket hydrogen bond, which appears to be stronger in the P115A mutant, may help retard the O₂ ligand from escaping into the solvent following either photoinduced or thermal dissociation. This, along with a strengthening of the Fe–O₂ bond that is correlated with the significant heme ruffing and saddling distortions, explains the unusually high O₂ affinity of WT Tt H-NOX and the even higher affinity found in the P115A mutant." @default.
• W3019972607 created "2020-05-01" @default.
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• W3019972607 date "2016-01-01" @default.
• W3019972607 modified "2023-09-23" @default.
• W3019972607 title "Kinetic Control of O2 Reactivity in H-NOX Domains B" @default.
• W3019972607 hasPublicationYear "2016" @default.
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