| Structural highlights
7dvo is a 2 chain structure with sequence from Cbs 144134. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| Gene: | CYP55A1, CYP55 (CBS 144134) |
| Activity: | Nitric oxide reductase (NAD(P)(+), nitrous oxide-forming), with EC number 1.7.1.14 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[NOR_FUSOX] Nitric oxide reductase which is involved in a dissimilatory reduction of nitrite. Acts as a nitric oxide reductase. Is able to reduce nitrate and nitrite to a gaseous form of N(2)O when oxygen supply is limited or discontinued. May function as a detoxification mechanism.[1] [2]
Publication Abstract from PubMed
Nitric oxide (NO) reductase from the fungus Fusarium oxysporum is a P450-type enzyme (P450nor) that catalyzes the reduction of NO to nitrous oxide (N2O) in the global nitrogen cycle. In this enzymatic reaction, the heme-bound NO is activated by the direct hydride transfer from NADH to generate a short-lived intermediate ( I ), a key state to promote N-N bond formation and N-O bond cleavage. This study applied time-resolved (TR) techniques in conjunction with photolabile-caged NO to gain direct experimental results for the characterization of the coordination and electronic structures of I TR freeze-trap crystallography using an X-ray free electron laser (XFEL) reveals highly bent Fe-NO coordination in I , with an elongated Fe-NO bond length (Fe-NO = 1.91 A, Fe-N-O = 138 degrees ) in the absence of NAD(+) TR-infrared (IR) spectroscopy detects the formation of I with an N-O stretching frequency of 1,290 cm(-1) upon hydride transfer from NADH to the Fe(3+)-NO enzyme via the dissociation of NAD(+) from a transient state, with an N-O stretching of 1,330 cm(-1) and a lifetime of ca. 16 ms. Quantum mechanics/molecular mechanics calculations, based on these crystallographic and IR spectroscopic results, demonstrate that the electronic structure of I is characterized by a singly protonated Fe(3+)-NHO(*-) radical. The current findings provide conclusive evidence for the N2O generation mechanism via a radical-radical coupling of the heme nitroxyl complex with the second NO molecule.
Short-lived intermediate in N2O generation by P450 NO reductase captured by time-resolved IR spectroscopy and XFEL crystallography.,Nomura T, Kimura T, Kanematsu Y, Yamada D, Yamashita K, Hirata K, Ueno G, Murakami H, Hisano T, Yamagiwa R, Takeda H, Gopalasingam C, Kousaka R, Yanagisawa S, Shoji O, Kumasaka T, Yamamoto M, Takano Y, Sugimoto H, Tosha T, Kubo M, Shiro Y Proc Natl Acad Sci U S A. 2021 May 25;118(21). pii: 2101481118. doi:, 10.1073/pnas.2101481118. PMID:34001620[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shoun H, Tanimoto T. Denitrification by the fungus Fusarium oxysporum and involvement of cytochrome P-450 in the respiratory nitrite reduction. J Biol Chem. 1991 Jun 15;266(17):11078-82. PMID:2040619
- ↑ Zhang L, Kudo T, Takaya N, Shoun H. The B' helix determines cytochrome P450nor specificity for the electron donors NADH and NADPH. J Biol Chem. 2002 Sep 13;277(37):33842-7. Epub 2002 Jul 8. PMID:12105197 doi:http://dx.doi.org/10.1074/jbc.M203923200
- ↑ Nomura T, Kimura T, Kanematsu Y, Yamada D, Yamashita K, Hirata K, Ueno G, Murakami H, Hisano T, Yamagiwa R, Takeda H, Gopalasingam C, Kousaka R, Yanagisawa S, Shoji O, Kumasaka T, Yamamoto M, Takano Y, Sugimoto H, Tosha T, Kubo M, Shiro Y. Short-lived intermediate in N2O generation by P450 NO reductase captured by time-resolved IR spectroscopy and XFEL crystallography. Proc Natl Acad Sci U S A. 2021 May 25;118(21). pii: 2101481118. doi:, 10.1073/pnas.2101481118. PMID:34001620 doi:http://dx.doi.org/10.1073/pnas.2101481118
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