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Our research concerns a fascinating group of proteins that contain complex clusters of metal ions and inorganic ligands at their active sites. These proteins play essential roles in such crucial biochemical processes as nitrogen fixation, photosynthesis, oxidative phosphorylation and ribonucleotide reduction. We aim to understand the relationship between the structures and catalytic mechanisms of enzymes that employ such clusters, and to elucidate the biochemical mechanisms by which the proteins acquire their clusters. Currently, the majority of our efforts are in two areas. In the first, we are defining structure-reactivity relationships among members of a large class of enzymes that use carboxylate-bridged dinuclear iron clusters (see Figure 1, top) to activate molecular oxygen for diverse oxidation reactions. Several of these reactions, which range from hydrocarbon hydroxylation (e.g. methane monooxygenase, MMO) to fatty acid desaturation (e.g. stearoyl acyl carrier protein delta-9 desaturase, delta-9-D) to generation of a stable tyrosyl radical (in subunit R2 of ribonucleotide reductase, R2-RNR), are considered to be difficult because no counterparts exist in the repertoire of the synthetic chemist, in spite of the significant effort that has been directed toward their development
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Papers共 224 篇Author StatisticsCo-AuthorSimilar Experts
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JOURNAL OF THE AMERICAN CHEMICAL SOCIETYno. 3 (2024): 1977-1983
Nunziata Maio,Md Kausar Raza,Yan Li, De-Liang Zhang,J Martin Bollinger,Carsten Krebs,Tracey A Rouault
Molly J McBride, Sarah R Pope,Mrutyunjay A Nair,Debangsu Sil, Xavier E Salas-Solá,Carsten Krebs,J Martin Bollinger,Amie K Boal
bioRxiv : the preprint server for biologyno. 16 (2023): 2480-2491
ACS CATALYSISno. 12 (2022): 6968-6979
ACS CATALYSISno. 12 (2022): 6968-6979
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