Work

Preparation of Non-heme {FeNO}7 Models of Cysteine Dioxygenase: Sulfur versus Nitrogen Ligation and Photorelease of Nitric Oxide

Year: 2013

Type: article

Abstract: We present the synthesis and spectroscopic characterization of [Fe(NO)(N3PyS)]BF4 (3), the first structural and electronic model of NO-bound cysteine dioxygenase. The nearly isostructural all-N-donor analogue [Fe(NO)(N4Py)](BF4)2 (4) was also prepared, and comparisons of 3 and 4 provide insight regarding the influence of S vs N ligation in {FeNO}(7) species. One key difference occurs upon photoirradiation, which causes the fully reversible release of NO from 3, but not from 4.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja4064487

Authors: Alison C. McQuilken, Yang Ha, Kyle D. Sutherlin, Maxime A. Siegler, Keith O. Hodgson, Britt Hedman, Edward I. Solomon, Guy N. L. Jameson, David P. Goldberg

Institutions: Johns Hopkins University, Stanford University, SLAC National Accelerator Laboratory, Stanford Synchrotron Radiation Lightsource, University of Otago, MacDiarmid Institute for Advanced Materials and Nanotechnology

Language: English

Topic: Metal-Catalyzed Oxygenation Mechanisms

Subfield: Inorganic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences

Awards: G2300450775, Synthetic Models of N/S-Ligated Metal Centers in Biology, G4200735206, G5010408774, Spectroscopic Characterization of Oxygen Intermediates in Non-heme and Heme Iron Enzymes, A Synchrotron Radiation Structural Biology Resource

OpenAlex ID: W2062373493

FWCI: 3.3

Cites: 44

Cited by: 70

Related to: 10