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Intramembrane Bis-Heme Motif for Transmembrane Electron Transport Conserved in a Yeast Iron Reductase and the Human NADPH Oxidase
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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.
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“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).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [288]
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Metadata
- 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
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › 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
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