Evidence map›Paper›PMID 22004125›Full record

ArticleBiochemistry2011

Manipulating cofactor binding thermodynamics in an artificial oxygen transport protein.

Lei Zhang, J L Ross Anderson, Ismail Ahmed, Jessica A Norman, Christopher Negron, Andrew C Mutter, P Leslie Dutton, Ronald L Koder

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

18 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Tailorable Tetrahelical Bundles as a Toolkit for Redox Studies.The journal of physical chemistry. B · 2022
    Article
  4. Liquid to solid transition of elastin condensates.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Article
  7. Designing heterotropically activated allosteric conformational switches using supercharging.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Preface.Methods in enzymology · 2016
    Article
  12. Review
  13. Engineering the assembly of heme cofactors in man-made proteins.Journal of the American Chemical Society · 2014
    Article
  14. Article
  15. Article
  16. Article
  17. Modulation of function in a minimalist heme-binding membrane protein.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012
    Article
  18. Article
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

8 authors at 2 institutions in 1 country.

Lei ZhangDepartment of Physics, The City College of New York, New York, New York 10031, United States.
J L Ross Anderson
Ismail Ahmed
Jessica A Norman
Christopher Negron
Andrew C Mutter
P Leslie Dutton
Ronald L Koder
City College of New York · USUniversity of Pennsylvania · US

Funding

TNC FUNCTION IN APOPTOTIC ANTIGEN DRIVEN AUTOIMMUNITYG12RR003060 · NCRR · CITY COLLEGE OF NEW YORK · PI WALLMAN, JOSHUA · 1985 to 2011
$26.1M
Cellular/Molecular Basis of Development: Research CenterG12MD007603 · NIMHD · CITY COLLEGE OF NEW YORK · PI PEZZANO, MARK · 2012 to 2017
$11.5M
Natural Engineering of Multi-Electron Biological Oxidation & ReductionR01GM041048 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DUTTON, PETER LESLIE · 1989 to 2014
$5.0M
900 MHz NMR Spectrometer for Structural BiologyP41GM066354 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI COWBURN, DAVID · 2002 to 2006
$4.7M
MARC HONORS UNDERGRADUATE RESEARCH TRAINING PROGRAMT34GM007639 · NIGMS · CITY COLLEGE OF NEW YORK · PI LEVITT, JONATHAN B · 1985 to 2022
$4.7M
NCRR NIH HHS 5G12 RR03060NCRR NIH HHS G12 RR003060NIGMS NIH HHS P41 GM066354NIGMS NIH HHS P41 GM-66354NIGMS NIH HHS R01 GM041048NIGMS NIH HHS R01GM41048NIGMS NIH HHS T34 GM007639NIMHD NIH HHS G12 MD007603
6 · The paper itself

Abstract

We report the mutational analysis of an artificial oxygen transport protein, HP7, which operates via a mechanism akin to that of human neuroglobin and cytoglobin. This protein destabilizes one of two heme-ligating histidine residues by coupling histidine side chain ligation with the burial of three charged glutamate residues on the same helix. Replacement of these glutamate residues with alanine, which is uncharged, increases the affinity of the distal histidine ligand by a factor of 13. Paradoxically, it also decreases heme binding affinity by a factor of 5 in the reduced state and 60 in the oxidized state. Application of a three-state binding model, in which an initial pentacoordinate binding event is followed by a protein conformational change to hexacoordinate, provides insight into the mechanism of this seemingly counterintuitive result: the initial pentacoordinate encounter complex is significantly destabilized by the loss of the glutamate side chains, and the increased affinity for the distal histidine only partially compensates for that. These results point to the importance of considering each oxidation and conformational state in the design of functional artificial proteins.

Indexed as

Genes, SyntheticAmino Acid SequenceBase SequenceHemeHemeproteinsHumansKineticsModels, MolecularMolecular Sequence DataOxidation-ReductionOxygenProtein BindingProtein EngineeringThermodynamicsHemeHemeproteinsOxygen

Identifiers

PMID22004125
PMCPMC3561710
OpenAlexW1990954580

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.