Zobrazeno 1 - 10 of 15 pro vyhledávání: '"D. M. Arciero"'
1
Low temperature EPR and Mossbauer spectroscopic of two cytochromes with His-Met axial coordination exhibiting HALS signals
Autor: G. Zoppellaro, T. Teschner, E. Harbtiz, V. Schunemann, S. Karlsen, D. M. Arciero, A. X. Trautwein, A. B. Hooper, K. K. Andersson, CIURLI, STEFANO LUCIANO
C-type cytochromes with histidine–methionine (His–Met) iron coordination play important roles in electron-transfer reactions and in enzymes. Low-temperature electron paramagnetic resonance (EPR) spectra of low-spin ferric cytochromes c can be div
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______4094::18aadc00cba4c2b63df39e5403142550
http://hdl.handle.net/11585/32711
Zobrazit plný text záznamu
2
Enzymology of the oxidation of ammonia to nitrite by bacteria
Autor: A B, Hooper, T, Vannelli, D J, Bergmann, D M, Arciero
Publikováno v: Antonie van Leeuwenhoek. 71(1-2)
The enzymes which catalyze the oxidation of ammonia to nitrite by autotrophic bacteria are reviewed. A comparison is made with enzymes which catalyze the same reactions in methylotrophs and organotrophic heterotrophic bacteria.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8044b64f8091f0cd8a499369ab4f61fe
https://pubmed.ncbi.nlm.nih.gov/9049018
Zobrazit plný text záznamu
3
A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states
Autor: D M, Arciero, A B, Hooper
Publikováno v: The Journal of biological chemistry. 269(16)
A di-c-heme containing cytochrome (cytochrome c553 peroxidase) has been isolated from the chemoautotrophic bacterium Nitrosomonas europaea. Sequence analysis of the N terminus and the two heme-containing peptides generated by digestion of the enzyme
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1155cc9c4f40caffa970144214a11e6a
https://pubmed.ncbi.nlm.nih.gov/8163487
Zobrazit plný text záznamu
4
Hydroxylamine oxidoreductase from Nitrosomonas europaea is a multimer of an octa-heme subunit
Autor: D M, Arciero, A B, Hooper
Publikováno v: The Journal of biological chemistry. 268(20)
A fully active form of hydroxylamine oxidoreductase from Nitrosomonas has been purified with high recovery and shown by reverse-phase high performance liquid chromatography and N-terminal analysis to contain only a 63-kDa subunit and to lack the 11-k
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bc17a7f5257c6893901ecb29a71d5f06
https://pubmed.ncbi.nlm.nih.gov/8325841
Zobrazit plný text záznamu
5
Optical spectropotentiometric resolution of the hemes of hydroxylamine oxidoreductase. Heme quantitation and pH dependence of Em
Autor: M J, Collins, D M, Arciero, A B, Hooper
Publikováno v: The Journal of biological chemistry. 268(20)
The hemes of hydroxylamine oxidoreductase (HAO) have been analyzed optically by potentiometric titrations using a low volume optically transparent thin layer electrochemical cell. The electrochemical behavior of the HAO monomeric unit has been interp
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1a26214eae400e30541c12b0eba7e4eb
https://pubmed.ncbi.nlm.nih.gov/8325842
Zobrazit plný text záznamu
7
In vitro attachment of bilins to apophycocyanin. III. Properties of the phycoerythrobilin adduct
Autor: D M Arciero, J L Dallas, Alexander N. Glazer
Publikováno v: Journal of Biological Chemistry. 263:18358-18363
Addition of phycoerythrobilin (PEB) to apophycocyanin at pH 7.0 resulted in covalent adduct formation. The adduct showed absorbance maxima at 575 and 605 nm and fluorescence emission maxima at 582 and 619 nm. Analysis of bilin peptides obtained upon
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e6d63b3c5e9c5dbb93d60aa75c642998
https://doi.org/10.1016/s0021-9258(19)81367-4
Zobrazit plný text záznamu
8
In vitro attachment of bilins to apophycocyanin. I. Specific covalent adduct formation at cysteinyl residues involved in phycocyanobilin binding in C-phycocyanin
Autor: D M Arciero, Donald A. Bryant, Alexander N. Glazer
Publikováno v: Journal of Biological Chemistry. 263:18343-18349
Expression of cloned alpha and beta subunit genes of Synechococcus sp. PCC7002 C-phycocyanin in Escherichia coli led to the production of large amounts of apophycocyanin. The apophycocyanin was purified to homogeneity and shown to be an alpha beta mo
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::152ca79efa26cc2cd59b71fe50f7689a
https://doi.org/10.1016/s0021-9258(19)81365-0
Zobrazit plný text záznamu
9
In vitro attachment of bilins to apophycocyanin. II. Determination of the structures of tryptic bilin peptides derived from the phycocyanobilin adduct
Autor: D M Arciero, Alexander N. Glazer, J L Dallas
Publikováno v: Journal of Biological Chemistry. 263:18350-18357
In vitro reaction of phycocyanobilin (PCB) with apophycocyanin results in the specific addition of the bilin to two of the cysteinyl residues, alpha-Cys-84 and beta-Cys-82, which normally function in PCB attachment (Arciero, D. M., Bryant, D. A., and
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e146048fc7d6dace081e4017a7ef6c57
https://doi.org/10.1016/s0021-9258(19)81366-2
Zobrazit plný text záznamu
10
Binding of 17O-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex. Evidence for direct substrate binding to the active site Fe2+ of extradiol dioxygenases
Autor: D M, Arciero, J D, Lipscomb
Publikováno v: The Journal of biological chemistry. 261(5)
Pseudomonas testosteroni protocatechuate 4,5-dioxygenase catalyzes extradiol-type oxygenolytic cleavage of the aromatic ring of its substrate. The essential active site Fe2+ binds nitric oxide (NO) to produce an EPR active complex with an electronic
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1e4b09f02b0b290365d8e3065e606b64
https://pubmed.ncbi.nlm.nih.gov/3003098
Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání

Omezení vyhledávání
Plný text Recenzováno Digitální knihovna AV ČR
Zdroje