The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Phthalate Dioxygenase Reductase: a Modular Structure for Electron Transfer from Pyridine Nucleotides to [2Fe-2S]
Abstract
Phthalate dioxygenase reductase (PDR) is a prototypical iron-sulfur flavoprotein (36 kilodaltons) that utilizes flavin mononucleotide (FMN) to mediate electron transfer from the two-electron donor, reduced nicotinamide adenine nucleotide (NADH), to the one-electron acceptor, [2Fe-2S]. The crystal structure of oxidized PDR from Pseudomonas cepacia has been analyzed at 2.0 angstrom resolution resolution; reduced PDR and pyridine nucleotide complexes have been analyzed at 2.7 angstrom resolution. NADH, FMN, and the [2Fe-2S] cluster, bound to distinct domains, are brought together near a central cleft in the molecule, with only 4.9 angstroms separating the flavin 8-methyl and a cysteine sulfur ligated to iron. The domains that bind FMN and [2Fe-2S] are packed so that the flavin ring and the plane of the [2Fe-2S] core are approximately perpendicular. The [2Fe-2S] group is bound by four cysteines in a site resembling that in plant ferredoxins, but its redox potential (-174 millivolts at pH 7.0) is much higher than the potentials of plant ferredoxins. Structural and sequence similarities assign PDR to a distinct family of flavoprotein reductases, all related to ferredoxin NADP + -reductase.
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Metadata
- Authors
- Correll, C. C., Batie, C. J., Ballou, D. P., & Ludwig, M. L.
- Venue
- Science
- Published
- 1992-12-04
- Volume
- 258
- Issue
- 5088
- Pages
- 1604-1610
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2074910209
- Cited by
- 296
- References
- 43
- FWCI
- 24.15
- Type
- journal article
- Language
- en
- Open access
- closed
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- Correll, C. C., Batie, C. J., Ballou, D. P., & Ludwig, M. L. (1992). Phthalate Dioxygenase Reductase: a Modular Structure for Electron Transfer from Pyridine Nucleotides to [2Fe-2S]. Science. https://doi.org/10.1126/science.1280857
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