期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 132, 期 27, 页码 9247-9249出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja1012273
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资金
- NASA Astrobiology Institute [NNA08CN85A]
- Air Force Office of Scientific Research
- NASA [103836, NNA08CN85A] Funding Source: Federal RePORTER
Biosynthesis of the unusual organometallic H-cluster at the active site of the [FeFe]-hydrogenase requires three accessory proteins, two of which are radical Ado Met enzymes (HydE, HydG) and one of which is a GTPase (HydF). We demonstrate here that HydG catalyzes the synthesis of CO using tyrosine as a substrate. CO production was detected by using deoxyhemoglobin as a reporter and monitoring the appearance of the characteristic visible spectroscopic features of carboxyhemoglobin. Assays utilizing C-13-tyrosine were analyzed by FTIR to confirm the production of HbCO and to demonstrate that the CO product was synthesized from tyrosine. CO ligation is a common feature at the active sites of the [FeFe], [NiFe], and [Fe]-only hydrogenases; however, this is the first report of the enzymatic synthesis of CO in hydrogenase maturation.
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