IMR Press / FBL / Volume 23 / Issue 10 / DOI: 10.2741/4678

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Review

Trapping methods for probing functional intermediates in nitric oxide synthases and related enzymes

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1 Manchester Institute of Biotechnology and School of Chemistry, The University of Manchester, Manchester, United Kingdom
Front. Biosci. (Landmark Ed) 2018, 23(10), 1874–1888; https://doi.org/10.2741/4678
Published: 1 June 2018
(This article belongs to the Special Issue Nitric oxide: Biology and chemistry)
Abstract

The three mammalian isoforms of nitric oxide synthase (NOS) produce the signalling molecule nitric oxide (NO) from L-arginine, molecular oxygen, and NADPH. NOS-generated NO is essential for many key biochemical processes and aberrant NO production is linked to the pathophysiology of many diseases. Over the past 40 years, the mechanism and structure of NOS have been studied extensively and there are many quality reviews and perspectives documenting the current hypotheses in the field. In this review, as an alternative perspective, we will describe some novel techniques and methodologies that have been used to trap functionally relevant conformational and kinetic states in the catalytic cycles of NOS and some structurally related diflavin oxidoreductase. The methods described in this perspective have enabled characterisation of the complex NOS and diflavin oxidoreductase family members (including cytochrome P450 reductase) and should find future application in other enzyme systems.

Keywords
Nitric Oxide Synthase
Trapping
Protein Domain Dynamics
Thermodynamic Block
Electron Transfer Chemistry
Review
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