Výsledky vyhledávání - "Carsten, Krebs"

Akademický článek

Heme biosynthesis depends on previously unrecognized acquisition of iron-sulfur cofactors in human amino-levulinic acid dehydratase

Autor: Gang Liu, Debangsu Sil, Nunziata Maio, Wing-Hang Tong, J. Martin Bollinger, Carsten Krebs, Tracey Ann Rouault

Publikováno v: Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)

Heme biosynthesis depends on iron-sulfur (Fe-S) cluster biogenesis but the molecular connection between these pathways is not fully understood. Here, the authors show that the heme biosynthesis enzyme ALAD contains an Fe-S cluster, disruption of whic

Externí odkaz: https://doaj.org/article/e72a170c1c0d4aa795c47a4475b86629

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What Is the Right Level of Activation of a High-Spin {FeNO}7 Complex to Enable Direct N–N Coupling? Mechanistic Insight into Flavodiiron NO Reductases

Autor: Hai T. Dong, Stephanie Camarena, Debangsu Sil, Michael O. Lengel, Jiyong Zhao, Michael Y. Hu, E. Ercan Alp, Carsten Krebs, Nicolai Lehnert

Publikováno v: J Am Chem Soc

Flavodiiron nitric oxide reductases (FNORs), found in pathogenic bacteria, are capable of reducing nitric oxide (NO) to nitrous oxide (N(2)O) to detoxify NO released by the human immune system. Previously, we reported the first FNOR model system that

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc2995106944b78bb73b7289ef8528d7
https://doi.org/10.1021/jacs.2c04292

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Synergistic Binding of the Halide and Cationic Prime Substrate of the l-Lysine 4-Chlorinase, BesD, in Both Ferrous and Ferryl States

Autor: Jeffrey W. Slater, Monica E. Neugebauer, Molly J. McBride, Debangsu Sil, Chi-Yun Lin, Bryce J. Katch, Amie K. Boal, Michelle C.Y. Chang, Alexey Silakov, Carsten Krebs, J. Martin Bollinger

Publikováno v: bioRxiv

An aliphatic halogenase requires four substrates: 2-oxoglutarate (2OG), halide (Cl−or Br−), the halogenation target (“prime substrate”), and dioxygen. In well-studied cases, the three non-gaseous substrates must bind to activate the enzyme’

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14b9fbd5470ea79412bbe4a20efb2a5d
https://doi.org/10.1101/2023.05.02.539147

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Substrate-Triggered μ-Peroxodiiron(III) Intermediate in the 4-Chloro-l-Lysine-Fragmenting Heme-Oxygenase-like Diiron Oxidase (HDO) BesC: Substrate Dissociation from, and C4 Targeting by, the Intermediate

Autor: Molly J. McBride, Mrutyunjay A. Nair, Debangsu Sil, Jeffrey W. Slater, Monica E. Neugebauer, Michelle C. Y. Chang, Amie K. Boal, Carsten Krebs, J. Martin Bollinger

Publikováno v: Biochemistry

The enzyme BesC from the β-ethynyl-L-serine biosynthetic pathway in Streptomyces cattleya fragments 4-chloro-L-lysine (produced from L-Lysine by BesD) to ammonia, formaldehyde, and 4-chloro-L-allylglycine and can analogously fragment L-Lys itself. B

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76f6540199357ff8469be639a7484ad9
https://doi.org/10.1021/acs.biochem.1c00774

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Capturing a bis-Fe(IV) State in Methylosinus trichosporium OB3b MbnH

Autor: Anastasia C. Manesis, Jeffrey W. Slater, Kenny Cantave, J. Martin Bollinger, Carsten Krebs, Amy C. Rosenzweig

Publikováno v: Biochemistry

The diheme bacterial cytochrome c peroxidase (bCcP)/MauG superfamily is a diverse set of enzymes that remains largely uncharacterized. One recently discovered member, MbnH, converts a tryptophan residue in its substrate protein, MbnP, to kynurenine.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6504117da0ffcc2c7714f596410e192d
https://europepmc.org/articles/PMC10083075/

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Structural basis for tRNA methylthiolation by the radical SAM enzyme MiaB

Autor: Arthur J. Arcinas, Tyler L. Grove, Bo Wang, Carsten Krebs, Neela H. Yennawar, Squire J. Booker, Olga Esakova, Steven C. Almo

Publikováno v: Nature

Numerous post-transcriptional modifications of transfer RNAs have vital roles in translation. The 2-methylthio-N6-isopentenyladenosine (ms2i6A) modification occurs at position 37 (A37) in transfer RNAs that contain adenine in position 36 of the antic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b4729a1e52020101398b27bc00e6964
https://doi.org/10.1038/s41586-021-03904-6

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In Vitro Demonstration of Human Lipoyl Synthase Catalytic Activity in the Presence of NFU1

Autor: Douglas M. Warui, Debangsu Sil, Kyung-Hoon Lee, Syam Sundar Neti, Olga A. Esakova, Hayley L. Knox, Carsten Krebs, Squire J. Booker

Publikováno v: ACS biomed chem Au. 2(5)

Lipoyl synthase (LS) catalyzes the last step in the biosynthesis of the lipoyl cofactor, which is the attachment of sulfur atoms at C6 and C8 of an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d66aa4221a8eee66c6588872b9862db
https://pubmed.ncbi.nlm.nih.gov/36281303

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