期刊
BULLETIN OF THE CHEMICAL SOCIETY OF JAPAN
卷 93, 期 7, 页码 825-833出版社
CHEMICAL SOC JAPAN
DOI: 10.1246/bcsj.20200038
关键词
Nitric oxide; Heme enzyme; Time-resolved spectroscopy
资金
- MEXT KAKENHI [26220807, 19H03171, 17H03092, 15H05476, 23687022, 17H06955, 18H02412]
- JSPS KAKENHI [19J15471]
- K-CONNEX
- RIKEN Pioneering Project Dynamic Structural Biology
- Grants-in-Aid for Scientific Research [17H03092, 19H03171, 19J15471, 26220807, 15H05476, 17H06955, 23687022, 18H02412] Funding Source: KAKEN
Membrane-integrated nitric oxide reductases (NOR) catalyze the formation of nitrous oxide (N2O) from two NO molecules using two protons and two electrons at a heme/non-heme iron binuclear center. Despite extensive efforts, the mechanism underlying the NOR-catalyzed reaction has been poorly understood due to the rapidity of the reaction. Here, we utilized a photosensitive caged NO compound as a trigger for the NOR reaction to characterize the NO reduction mechanism by time-resolved visible absorption spectroscopy. We showed that the NOR reaction consists of three steps. One NO molecule binds to the reduced binuclear center to form a non-heme Fe(II)-NO species in the 1st phase (microsecond timescale), followed by a migration of NO to form the other chemical species, possibly 5-coordinate heme b(3)-NO, in the 2nd phase (timescale of tens of microseconds). Then, the NO bound to heme reacts with a second NO molecule in the 3rd phase (millisecond timescale), in which protonation and electron transfer promote N-N bond formation and N-O bond cleavage to yield N2O. These findings led us to propose a revised trans mechanism for NO reduction by NOR.
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