Evidence map›Paper›PMID 27686338›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2016

Exploring second coordination sphere effects in nitric oxide synthase.

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

Open access · greenAbstract read
In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 8 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Ashley B McQuartersDepartment of Chemistry, University of Michigan, Ann Arbor, MI, 48109, USA.
Amy L SpeelmanDepartment of Chemistry, University of Michigan, Ann Arbor, MI, 48109, USA.
Li ChenCollege of Pharmacy, University of New Mexico, Albuquerque, NM, 87131, USA.
Bradley O ElmoreCollege of Pharmacy, University of New Mexico, Albuquerque, NM, 87131, USA.
Weihong FanCollege of Pharmacy, University of New Mexico, Albuquerque, NM, 87131, USA.
Changjian FengCollege of Pharmacy, University of New Mexico, Albuquerque, NM, 87131, USA.
Nicolai LehnertDepartment of Chemistry, University of Michigan, Ann Arbor, MI, 48109, USA. lehnertn@umich.edu.
University of New Mexico · USUniversity of Michigan–Ann Arbor · US

Funding

Mechanisms of Electron Transfer in Nitric Oxide Synthases: the Output State in NiR15GM081811 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI FENG, CHANGJIAN · 2007 to 2016
$1.0M
NIGMS NIH HHS R15 GM081811
6 · The paper itself

Abstract

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 regulate the Fe-S interaction. Previous work identified the S(Cys) → Fe σ CT transition in the high-spin (hs) ferric form of Cyt P450cam and corresponding Cys pocket mutants by low-temperature (LT) MCD spectroscopy [Biochemistry 50:1053, 2011]. In this work, we have investigated the effect of the hydrogen bond from W409 to the axial Cys ligand of the heme in the hs ferric state (with H

Indexed as

Catalytic DomainAnimalsBinding SitesCircular DichroismCoordination ComplexesCysteineCytochrome P-450 Enzyme SystemHemeHydrogen BondingIronLigandsModels, MolecularMutationNitric OxideNitric Oxide Synthase Type IOxidation-ReductionCoordination ComplexesCysteineCytochrome P-450 Enzyme SystemHemeIronLigandsNitric OxideNitric Oxide Synthase Type ICytochrome P450Electronic SpectraHemeMagnetic circular dichroismNitric oxide synthaseSecond coordination sphere effects

Identifiers

PMID27686338
PMCPMC5541774
OpenAlexW2524767334

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.