Výsledky vyhledávání

Akademický článek

Recent Insights into the Reaction Mechanisms of Non-Heme Diiron Enzymes Containing Oxoiron(IV) Complexes.

Autor: Li RN; Key Laboratory of Cluster Science of Ministry of Education, School of Chemistry and Chemical Engineering, Beijing Institute of Technology, Beijing, 100081, China., Chen SL; Key Laboratory of Cluster Science of Ministry of Education, School of Chemistry and Chemical Engineering, Beijing Institute of Technology, Beijing, 100081, China.

Publikováno v: Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Nov 07, pp. e202400788. Date of Electronic Publication: 2024 Nov 07.

Zobrazit plný text záznamu

Akademický článek

Integrated Solution for As(III) Contamination in Water Based on Crystalline Porous Organic Salts.

Autor: Yang, Xiaoxia¹, Guo, Qi¹, Liu, Xingman¹, Ma, Jing‐xin¹ majing_xin@nxu.edu.cn

Publikováno v: Advanced Science. 8/27/2024, Vol. 11 Issue 32, p1-12. 12p.

Zobrazit plný text záznamu

Plný text ve formátu HTML

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

Akademický článek

Tutorial Review on the Set-Up and Running of Quantum Mechanical Cluster Models for Enzymatic Reaction Mechanisms.

Autor: de Visser SP; Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom.; Department of Chemical Engineering, The University of Manchester, Oxford Road, Manchester, M13 9PL, United Kingdom.; Department of Chemistry, Indian Institute of Technology Guwahati, Assam, 781039, India., Wong HPH; Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom.; Department of Chemical Engineering, The University of Manchester, Oxford Road, Manchester, M13 9PL, United Kingdom., Zhang Y; Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom.; Department of Chemical Engineering, The University of Manchester, Oxford Road, Manchester, M13 9PL, United Kingdom., Yadav R; Department of Chemistry, Indian Institute of Technology Guwahati, Assam, 781039, India., Sastri CV; Department of Chemistry, Indian Institute of Technology Guwahati, Assam, 781039, India.

Publikováno v: Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2024 Oct 28; Vol. 30 (60), pp. e202402468. Date of Electronic Publication: 2024 Oct 07.

Zobrazit plný text záznamu

Integrity of thermus thermophilus cytochrome c552 synthesized by Escherichia coli cells expressing the host-specific cytochrome c maturation genes, ccmABCDEFGH: biochemical, spectral, and structural characterization of the recombinant protein

Autor: J A, Fee, Y, Chen, T R, Todaro, K L, Bren, K M, Patel, M G, Hill, E, Gomez-Moran, T M, Loehr, J, Ai, L, Thöny-Meyer, P A, Williams, E, Stura, V, Sridhar, D E, McRee

Publikováno v: Protein science : a publication of the Protein Society. 9(11)

We describe the design of Escherichia coli cells that synthesize a structurally perfect, recombinant cytochrome c from the Thermus thermophilus cytochrome c552 gene. Key features are (1) construction of a plasmid-borne, chimeric cycA gene encoding an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4aafc3d2e3a94d83556eaeb770170c5f
https://pubmed.ncbi.nlm.nih.gov/11152119

Zobrazit plný text záznamu

Resonance Raman studies of Escherichia coli cytochrome bd oxidase. Selective enhancement of the three heme chromophores of the 'as-isolated' enzyme and characterization of the cyanide adduct

Autor: J, Sun, J P, Osborne, M A, Kahlow, T M, Kaysser, J J, Hil, R B, Gennis, T M, Loehr

Publikováno v: Biochemistry. 34(38)

Cytochrome bd oxidase is a terminal bacterial oxidase containing three cofactors: a low-spin heme (b558), a high-spin heme (b595), and a chlorin d. The center of dioxygen reduction has been proposed to be at a dinuclear b595/d site, whereas b558 is m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d930b6339066486b9dc322909153358
https://pubmed.ncbi.nlm.nih.gov/7547954

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání