Nitrosocyanin, a Red Cupredoxin-like Protein from Nitrosomonas europaea
| العنوان: | Nitrosocyanin, a Red Cupredoxin-like Protein from Nitrosomonas europaea |
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| المؤلفون: | David M. Arciero, Brad S. Pierce, Alan B. Hooper, Michael P. Hendrich |
| المصدر: | Biochemistry. 41:1703-1709 |
| بيانات النشر: | American Chemical Society (ACS), 2002. |
| سنة النشر: | 2002 |
| مصطلحات موضوعية: | DNA, Bacterial, Copper protein, Stereochemistry, Molecular Sequence Data, Biochemistry, Protein structure, Bacterial Proteins, Nitrosomonas europaea, Metalloproteins, Rusticyanin, Amino Acid Sequence, Cloning, Molecular, Nitrosomonas, Plastocyanin, Protein Structure, Quaternary, Peptide sequence, Base Sequence, Sequence Homology, Amino Acid, biology, Electron Spin Resonance Spectroscopy, biology.organism_classification, Nitrite reductase, Molecular Weight, Genes, Bacterial, Spectrophotometry, Azurin, Oxidoreductases, Copper |
| الوصف: | Nitrosocyanin (NC), a soluble, red Cu protein isolated from the ammonia-oxidizing autotrophic bacterium Nitrosomonas europaea, is shown to be a homo-oligomer of 12 kDa Cu-containing monomers. Oligonucleotides based on the amino acid sequence of the N-terminus and of the C-terminal tryptic peptide were used to sequence the gene by PCR. The translated protein sequence was significantly homologous with the mononuclear cupredoxins such as plastocyanin, azurin, or rusticyanin, the type 1 copper-binding region of nitrite reductase, and the binuclear CuA binding region of N(2)O reductase or cytochrome oxidase. The gene for NC contains a leader sequence indicating a periplasmic location. Optical bands for the red Cu center at 280, 390, 500, and 720 nm have extinction coefficients of 13.9, 7.0, 2.2, and 0.9 mM(-1), respectively. The reduction potential of NC (85 mV vs SHE) is much lower than those for known cupredoxins. Sequence alignments with homologous blue copper proteins suggested copper ligation by Cys95, His98, His103, and Glu60. Ligation by these residues (and a water), a trimeric protein structure, and a cupredoxin beta-barrel fold have been established by X-ray crystallography of the protein [Lieberman, R. L., Arciero, D. M., Hooper, A. B., and Rosenzweig, A. C. (2001) Biochemistry 40, 5674-5681]. EPR spectra of the red copper center indicated a Cu(II) species with a g(parallel) of 2.25 and an A(parallel) of 13.8 mT (144 x 10(-4) cm(-1)), typical of Cu in a type 2 copper environment. NC is the first example of a type 2 copper center in a cupredoxin fold. The open coordination site and type 2 copper suggest a possible catalytic rather than electron transfer function. |
| تدمد: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi015908w |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f50dda362726ccbe4b666398df952435 https://doi.org/10.1021/bi015908w |
| رقم الانضمام: | edsair.doi.dedup.....f50dda362726ccbe4b666398df952435 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15204995 00062960 |
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| DOI: | 10.1021/bi015908w |