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Hydroxylamine oxidoreductase from Nitrosomonas europaea is a multimer of an octa-heme subunit
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Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
4 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.
The 28 checked references that resolve
resolves10.1016/0014-5793(83)80292-0
O<sub>2</sub> and H<sub>2</sub>O are each the source of one O in NO<sup>−</sup><sub>2</sub> produced from NH<sub>3</sub> by <i>Nitrosomonas</i>: <sup>15</sup>N‐NMR evidence
resolves10.1016/S0021-9258(18)97148-6
Characterization of Hydroxylamine-Cytochrome c Reductase from the Chemoautotrophs Nitrosomonas europaea and Nitrosocystis oceanus
resolves10.1093/oxfordjournals.jbchem.a130510
Cytochrome c-552 and Cytochrome c-554 Derived from Nitrosomonas europaea
resolves10.1021/bi00112a014
Spectroscopic and rapid kinetic studies of reduction of cytochrome c554 by hydroxylamine oxidoreductase from Nitrosomonas europaea
resolves10.1021/bi00527a039
Hydroxylamine oxidoreductase: a 20-heme, 200,000 molecular weight cytochrome c with unusual denaturation properties which forms a 63,000 molecular weight monomer after heme removal
resolves10.1021/bi00608a007
Hydroxylamine oxidoreductase from Nitrosomonas: absorption spectra and content of heme and metal
resolves10.1016/0005-2728(72)90044-8
Preliminary characterization of a variant co-binding heme protein from Nitrosomonas
resolves10.1016/S0021-9258(17)39803-4
Mössbauer, EPR, and optical studies of the P-460 center of hydroxylamine oxidoreductase from Nitrosomonas. A ferrous heme with an unusually large quadrupole splitting.
resolves10.1016/0006-291X(91)90528-F
P460 of hydroxylamine oxidoreductase of Nitrosomonas europaea: Soret resonance Raman evidence for a novel heme-like structure
resolves10.1093/oxfordjournals.jbchem.a132604
Highly Purified Hydroxylamine Oxidoreductase Derived from Nitrosomonas europaea: Some Physicochemical and Enzymatic Properties1
resolves10.1021/bi00841a046
Hydroxylamine metabolism of Nitrosomonas europaea. II. Molecular properties of the electron-transport particle, hydroxylamine oxidase
resolves10.1002/elps.1150110205
Electrophoresis at elevated hydrostatic pressure of the multiheme hydroxylamine oxidoreductase
resolves10.1016/0014-5793(73)80756-2
Reaction of sulfenyl halides with cytochrome <i>c</i>. A novel method for heme cleavage
resolves10.1021/bi00260a011
Resolution of multiple heme centers of hydroxylamine oxidoreductase from Nitrosomonas. 2. Moessbauer spectroscopy
resolves10.1016/0014-5793(83)81154-5
Resolution of the hemes of hydroxylamine oxidoreductase by redox potentiometry and optical spectroscopy
resolves10.1021/bi00260a010
Resolution of multiple heme centers of hydroxylamine oxidoreductase from Nitrosomonas. 1. Electron paramagnetic resonance spectroscopy
resolves10.1021/bi00377a043
Resolution of the hemes of hydroxylamine oxidoreductase by redox potentiometry and electron spin resonance spectroscopy
resolves10.1111/j.1432-1033.1984.tb08230.x
Kinetics of reduction by substrate or dithionite and heme-heme electron transfer in the multiheme hydroxylamine oxidoreductase
resolves10.1038/227680a0
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
resolves10.1042/bj1090047Pb
The amino acid sequence of cytochrome c3 from Desulfovibrio vulgaris. (N.C. I.B. 8303)
resolves10.1016/0014-5793(69)80308-X
The structure of cytochrome <i>c</i>′<sub>3</sub> from desulfovibrio gigas (NCIB 9332)
resolves10.1021/ja00242a069
Synthesis and characterization of five-coordinate high-spin iron(II) porphyrin complexes with unusually large quadrupole splittings. Models for the P460 center of hydroxylamine oxidoreductase from Nitrosomonas
resolves10.1016/0014-5793(72)80220-5
The amino acid sequence of a cytochrome<i>c</i> from a protozoan<i>Crithidia oncopelti</i>
resolves10.1111/j.1432-1033.1975.tb02298.x
Evidence for the Amino-Acid Sequence of Crithidia fasciculata Cytochrome c555
resolves10.1038/241533a0
The Properties and Amino-acid Sequence of Cytochrome c from Euglena gracilis
The 4 references without a DOI — listed, not checked
no DOI — not checked10.1016/S0021-9258(18)82382-1_bib1
no DOI — not checked10.1016/S0021-9258(18)82382-1_bib16
no DOI — not checked10.1016/S0021-9258(18)82382-1_bib23
no DOI — not checked10.1016/S0021-9258(18)82382-1_bib24
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