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Article

Exploring second coordination sphere effects in nitric oxide synthase.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry - 1 Dec 2016

McQuarters Ashley B, Speelman Amy L, Chen Li, Elmore Bradley O, Fan Weihong, Feng Changjian, Lehnert Nicolai

Abstract excerpt

Second coordination sphere (SCS) effects in proteins are modulated by active site residues and include hydrogen bonding, electrostatic/dipole interactions, steric interactions, and π-stacking of aromatic residues. In Cyt P450s, extended H-bonding networks are located around the proximal cysteinate ligand of the heme, referred to as the 'Cys pocket'. These hydrogen bonding networks are generally believed to...

Topics

Animals
Binding Sites
Catalytic Domain
Circular Dichroism
Coordination Complexes
Cysteine
Cytochrome P-450 Enzyme System
Heme
Hydrogen Bonding
Iron

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Ligands

Models, Molecular

Mutation

Nitric Oxide

Nitric Oxide Synthase Type I

Oxidation-Reduction

Rats

Spectrophotometry

Source

Open in PubMed Open full text

Identifiers

PMID: 27686338
DOI: 10.1007/s00775-016-1396-1
PMCID: PMC5541774

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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