Cited by 214Metalloenzymes and iron-sulfur proteinsMetal-Catalyzed Oxygenation MechanismsHemoglobin structure and function

Intramembrane Bis-Heme Motif for Transmembrane Electron Transport Conserved in a Yeast Iron Reductase and the Human NADPH Oxidase

Open access
Finegold, Alan A., Shatwell, Karolyn P., Segal, Anthony W., Klausner, Richard D., Dancis, Andrew·1996·Journal of Biological Chemistry

Abstract

A plasma membrane iron reductase, required for cellular iron acquisition by Saccharomyces cerevisiae, and the human phagocytic NADPH oxidase, implicated in cellular defense, contain low potential plasma membrane b cytochromes that share elements of structure and function. Four critical histidine residues in the FRE1 protein of the iron reductase were identified by site-directed mutagenesis. Individual mutation of each histidine to alanine eliminated the entire heme spectrum without affecting expression of the apoprotein, documenting the specificity of the requirement for the histidine residues. These critical residues are predicted to coordinate a bis-heme structure between transmembrane domains of the FRE1 protein. The histidine residues are conserved in the related gp91(phox) protein of the NADPH oxidase of human granulocytes, predicting the sites of heme coordination in that protein complex. Similarly spaced histidine residues have also been implicated in heme binding by organelle b cytochromes with little overall sequence similarity to the plasma membrane b cytochromes. This bis-heme motif may play a role in transmembrane electron transport by distinct families of polytopic b cytochromes.

Integrity signals

Registry

Crossref · 10.1074/jbc.271.49.31021

Cites

27 of 27 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • The transmembrane domain includes four conserved histidines that serve as binding sites for two heme moieties bound between helices III and V.

    “The transmembrane domain includes four conserved histidines that serve as binding sites for two heme moieties bound between helices III and V (288, 613), and the flavoprotein domain binds the cofactor FAD and includes a binding site for NADPH (49, 480, 613, 980).”

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Finegold, A. A., Shatwell, K. P., Segal, A. W., Klausner, R. D., & Dancis, A.
Affiliations
  • National Institutes of Health (US)
  • University College London (GB)
Corresponding author
Dancis, Andrew
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1996-12
Volume
271
Issue
49
Pages
31021-31024
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2060193350
Cited by
213
References
27
Citations by year
2026: 3 · 2025: 1 · 2024: 5 · 2023: 6 · 2022: 3 · 2021: 7 · 2020: 3 · 2019: 9 · 2018: 6 · 2017: 2 · 2016: 5 · 2015: 4 · 2014: 8 · 2013: 5 · 2012: 2
FWCI
16.04
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
Wellcome Trust
Topics
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
Keywords
iron reductase, NADPH oxidase, gp91phox, heme coordination, histidine residues, Saccharomyces cerevisiae, human granulocytes, iron acquisition, site-directed mutagenesis
MeSH terms
Alleles, Amino Acid Sequence, Cytochrome b Group, Electron Transport, Heme, Humans, Models, Chemical, Molecular Sequence Data, NADH, NADPH Oxidoreductases, Saccharomyces cerevisiae, Sequence Alignment, NADPH Oxidases, FMN Reductase

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review