Výsledky vyhledávání - "J Sanders-Loehr"

X-ray Structure Determination and Characterization of the Pseudomonas aeruginosa Azurin Mutant Met121Glu

Autor: Herbert Nar, L.-C. Tsai, Lennart Sjölin, Langer, J. Sanders-Loehr, B.G. Karlsson, Nicklas Bonander

Publikováno v: Biochemistry. 36:4089-4095

The Met121Glu azurin mutant has been crystallized and the structure determined at a resolution of 2.3 A. In the crystal structure a carboxyl oxygen of Met121Glu is coordinated to the metal at a distance of 2.2 A. Single-crystal resonance Raman spectr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac8fd533d6bd8951fccb8f3dcf251aae
https://doi.org/10.1021/bi962416o

Zobrazit plný text záznamu

Dioxygen is the source of the mu-oxo bridge in iron ribonucleotide reductase

Autor: J. Ling, M. Sahlin, B.M. Sjöberg, T.M. Loehr, J. Sanders-Loehr

Publikováno v: Journal of Biological Chemistry. 269:5595-5601

The formation of the iron-radical cofactor in the R2 subunit of ribonucleotide reductase has been monitored by resonance Raman spectroscopy. The differrous cluster in reduced R2 functions as a tyrosine oxidase; it uses O2 to oxidize Tyr-122 to a stab

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d84f8ac562262938cab3b23176028ccb
https://doi.org/10.1016/s0021-9258(17)37503-8

Zobrazit plný text záznamu

Isolation, characterization, and amino acid sequences of auracyanins, blue copper proteins from the green photosynthetic bacterium Chloroflexus aurantiacus

Autor: J Han, G Tollin, Daniel C. Brune, T E Meyer, Robert E. Blankenship, J Sanders-Loehr, J D McManus, M A Cusanovich

Publikováno v: Journal of Biological Chemistry. 267:6531-6540

Three small blue copper proteins designated auracyanin A, auracyanin B-1, and auracyanin B-2 have been isolated from the thermophilic green gliding photosynthetic bacterium Chloroflexus aurantiacus. All three auracyanins are peripheral membrane prote

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::58436fd605c71fa760affed8ee248385
https://doi.org/10.1016/s0021-9258(19)50460-4

Zobrazit plný text záznamu

Peroxodiferric intermediate of stearoyl-acyl carrier protein delta 9 desaturase: oxidase reactivity during single turnover and implications for the mechanism of desaturation

Autor: Brian G. Fox, J. Sanders-Loehr, Jingyuan Ai, T. M. Loehr, John A. Broadwater

Publikováno v: Biochemistry. 37(42)

Combined optical and resonance Raman studies have revealed the formation of an O2-adduct upon exposure of 4e- chemically reduced stearoyl-acyl carrier protein Delta9 desaturase to stearoyl-ACP and 1 atm O2. The observed intermediate has a broad absor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9d93e85ce1844763da7cd238ce9f602
https://pubmed.ncbi.nlm.nih.gov/9778341

Zobrazit plný text záznamu

Techniques for obtaining resonance Raman spectra of metalloproteins

Autor: T M, Loehr, J, Sanders-Loehr

Publikováno v: Methods in enzymology. 226

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6eddd9c654dfb50da7c7f343ec6a34c3
https://pubmed.ncbi.nlm.nih.gov/8277876

Zobrazit plný text záznamu

Engineering of the iron site in ribonucleotide reductase to a self-hydroxylating monooxygenase

Autor: M, Ormö, F, deMaré, K, Regnström, A, Aberg, M, Sahlin, J, Ling, T M, Loehr, J, Sanders-Loehr, B M, Sjöberg

Publikováno v: The Journal of biological chemistry. 267(13)

Protein R2 of ribonucleotide reductase contains a dinuclear ferric iron center adjacent to a tyrosyl radical in the interior of the protein matrix. A patch of hydrophobic residues surrounds the iron-radical cofactor. Its importance during the oxidati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cbeadfa1f33bcc3b49c1fe2d21dd1fc7
https://pubmed.ncbi.nlm.nih.gov/1577712

Zobrazit plný text záznamu

Cloning of the vaccinia virus ribonucleotide reductase small subunit gene. Characterization of the gene product expressed in Escherichia coli

Autor: M L, Howell, J, Sanders-Loehr, T M, Loehr, N A, Roseman, C K, Mathews, M B, Slabaugh

Publikováno v: The Journal of biological chemistry. 267(3)

During its infectious cycle, vaccinia virus expresses a virus-encoded ribonucleotide reductase which is distinct from the host cellular enzyme (Slabaugh, M.B., and Mathews, C.K. (1984) J. Virol. 52, 501-506; Slabaugh, M.B., Johnson, T.L., and Mathews

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::aacb3e4c8e1b56b5e744ee4beb0dda0d
https://pubmed.ncbi.nlm.nih.gov/1309792

Zobrazit plný text záznamu

Biosynthesis of topa quinone cofactor in bacterial amine oxidases. Solvent origin of C-2 oxygen determined by Raman spectroscopy

Autor: N, Nakamura, R, Matsuzaki, Y H, Choi, K, Tanizawa, J, Sanders-Loehr

Publikováno v: Journal of Biological Chemistry. 271:9172

Resonance Raman spectroscopy is an excellent technique for providing structural information on the 2,4, 5-trihydroxyphenylalanine quinone (TPQ) cofactor in copper-containing amine oxidases. This technique has been used to investigate the copper- and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b00e97a2a7fc1bbf7d6fab8a0f525288
https://doi.org/10.1016/s0021-9258(17)35519-9

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání