Article
Chemistry, Multidisciplinary
Olivia M. Manley, Haoyu Tang, Shan Xue, Yisong Guo, Wei-chen Chang, Thomas M. Makris
Summary: BesC is a member of an emerging family of diiron enzymes that catalyze an unusual type of carbon-carbon cleavage reaction. It activates O-2 in a substrate-gated manner to generate a diferric-peroxo intermediate, initiating a unique reaction trajectory by cleaving the C4-H bond as the rate-limiting step in a single turnover reaction.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2021)
Article
Chemistry, Inorganic & Nuclear
Williamson N. Oloo, Miklos Szavuly, Jozsef Kaizer, Lawrence Que
Summary: This study describes a substrate oxidation reaction catalyzed by [Fe-II(IndH)(CH3CN)(3)](ClO4)(2) with H2O2, involving a spectroscopically characterized intermediate capable of olefin epoxidation and alkane hydroxylation. The research identified a direct nucleophilic attack of the substrate carbonyl group by the peroxo species. Additionally, the study found that the high-valent iron-oxo oxidant derived from O-O bond cleavage of the peroxo intermediate contributes to the oxidative reactivities associated with nonheme diiron enzymes.
INORGANIC CHEMISTRY
(2022)
Article
Chemistry, Physical
Yuan-Yang Guo, Ze-Hua Tian, Luying Wang, Zheng-De Lai, Lingjun Li, Yong-Quan Li
Summary: This study reports a chemoenzymatic method for the synthesis of phenol diarylamines, which can be performed in aqueous solutions. The method shows a broad substrate tolerance for phenol and aniline substrates. The study also highlights the synthetic potential of non-heme diiron N-oxygenases.
Article
Chemistry, Inorganic & Nuclear
Patrik Torok, Duenpen Unjaroen, Flora Viktoria Csendes, Michel Giorgi, Wesley R. Browne, Jozsef Kaizer
Summary: The complex [FeIII2(mu-O-2)(L-3)(4)(S)(2)](4+) is a functional model of peroxo-diiron intermediates in oxidoreductase catalytic cycles, exhibiting nucleophilic, electrophilic oxidative reactivity, and electron transfer oxidation.
DALTON TRANSACTIONS
(2021)
Article
Chemistry, Inorganic & Nuclear
Shiqing Zhang, Xinyi Li, Yijing Wang, Lijuan Yan, Jingjing Wei, Yongjun Liu
Summary: PtmU3 is a newly identified nonheme diiron monooxygenase with a special active site structure that can incorporate both atoms of a dioxygen molecule into substrates through successive reactions.
INORGANIC CHEMISTRY
(2021)
Review
Biochemistry & Molecular Biology
Joseana de Oliveira, Marina B. Denadai, Diego L. Costa
Summary: Heme oxygenase-1 (HO-1) plays a crucial role in iron metabolism and has the potential to modulate immunity and inflammation through regulating cellular oxidation reactions and the expression of inflammation-related proteins.
Article
Endocrinology & Metabolism
Wang Liao, Wanbao Yang, Zheng Shen, Weiqi Ai, Quan Pan, Yuxiang Sun, Shaodong Guo
Summary: This study elucidates the mechanism by which HO1 promotes gluconeogenesis in the liver, by increasing ferrous iron generation through HO1 overexpression to activate NF-κB and enhance gluconeogenesis. The importance of HO1 in insulin-resistant liver and the promotion of gluconeogenesis by systemic iron overload have been confirmed by the research.
Article
Chemistry, Multidisciplinary
Xiaodong Hou, Huibin Xu, Zhiwei Deng, Yijun Yan, Zhenbo Yuan, Xuanzhong Liu, Zengping Su, Sai Yang, Yan Zhang, Yijian Rao
Summary: This study identified the biosynthetic gene cluster of beticolin 1 in Cercospora using light-mediated comparative transcriptomics. It also discovered a novel non-heme iron oxygenase, BTG13, which is responsible for anthraquinone ring cleavage. The study provides important updates to our understanding of metalloenzymes.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2022)
Article
Chemistry, Inorganic & Nuclear
Bapan Samanta, Riya Ghosh, Rakesh Mazumdar, Shankhadeep Saha, Sayani Maity, Biplab Mondal
Summary: Researchers synthesized a Co(II) complex with a bidentate ligand and observed the corresponding transient intermediate through experiments. This study is important for understanding the reaction mechanism of the complex.
DALTON TRANSACTIONS
(2023)
Article
Biochemistry & Molecular Biology
Isabelle Fix, Lorenz Heidinger, Thorsten Friedrich, Gunhild Layer
Summary: In archaea and sulfate-reducing bacteria, heme is synthesized via the siroheme-dependent pathway. The Radical SAM enzyme AhbD catalyzes the last step of this pathway, converting iron-coproporphyrin III into heme. Amino acid sequence analysis and structural modeling suggested that some AhbD proteins may contain two auxiliary iron-sulfur clusters. Study on AhbD from Methanosarcina barkeri confirmed the presence of two auxiliary [4Fe-4S] clusters, and the clusters likely participate in the heme synthase activity.
Article
Chemistry, Multidisciplinary
Anja Greule, Thierry Izore, Daniel Machell, Mathias H. Hansen, Melanie Schoppet, James J. De Voss, Louise K. Charkoudian, Ralf B. Schittenhelm, Jeffrey R. Harmer, Max J. Cryle
Summary: Cytochrome P450 enzymes are enzymes that can perform oxidative reactions using heme. However, some of these enzymes can be damaged by oxidation, leading to decreased enzyme activity. Research has shown that the heme orientation in the active site of certain cytochrome P450 enzymes may contribute to this oxidative damage.
FRONTIERS IN CHEMISTRY
(2022)
Article
Chemistry, Multidisciplinary
Justin T. Henthorn, George E. Cutsail, Thomas Weyhermueller, Serena DeBeer
Summary: This article investigates the electronic structure and spin states of mixed-valent iron-sulfur dimers and discovers a new interaction that can stabilize high spin states. By studying a series of mixed-valent complexes, complex interactions between antiferromagnetic coupling, Heisenberg double-exchange, and vibronic coupling are revealed.
Letter
Chemistry, Multidisciplinary
Lixin Zhang, Xueting Liu, Xinye Wang, Guoliang Zhu, Heng Song, Ronghai Cheng, Nathchar Naowarojna, Catherine E. E. Costello, Pinghua Liu
Summary: In their recent publication, Cen, Wang, Zhou et al. reported the crystal structure of a ternary complex of the non-heme iron endoperoxidase FtmOx1 and concluded that it supports the CarC-like mechanistic model for catalysis. However, they failed to accurately describe the CarC-like and COX-like models and address their differences, and their data is consistent with the COX-like model after careful analysis.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2023)
Article
Chemistry, Multidisciplinary
Lian Wu, Zhanfeng Wang, Yixin Cen, Binju Wang, Jiahai Zhou
Summary: The high-resolution X-ray crystal structure of the ternary complex FtmOx1 center dot 2OG center dot fumitremorgin B and its catalytic mechanism were reported. In response to criticism from Zhang, Costello, Liu et al., the authors address their questions and provide structural clarifications and new computational results that support the CarC-like mechanistic model.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2023)
Article
Biochemistry & Molecular Biology
Xiaoyu Wang, Meiyin Wan, Lei Zhang, Yongdong Dai, Yang Hai, Chenda Yue, Junqi Xu, Yadan Ding, Mei Wang, Jianping Xie, Xia Lei, Julia-Li Zhong
Summary: This study investigated the efficacy of ALA_PDT against M. abscessus infections and found that it can kill M. abscessus by promoting ferroptosis-like death and oxidative stress through changes in iron metabolism. Additionally, ALA_PDT disrupted the integrity of the cell membrane and enhanced its permeability. These findings provide new mechanistic insights into the clinical treatment of M. abscessus using ALA_PDT.
Article
Chemistry, Inorganic & Nuclear
Katlyn K. Meier, Melanie S. Rogers, Elena G. Kovaleva, John D. Lipscomb, Emile L. Bominaar, Eckard Munck
INORGANIC CHEMISTRY
(2016)
Article
Chemistry, Multidisciplinary
Rebeca G. Castillo, Rahul Banerjee, Caleb J. Allpress, Gregory T. Rohde, Eckhard Bill, Lawrence Que, John D. Lipscomb, Serena DeBeer
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2017)
Article
Chemistry, Multidisciplinary
Andrew J. Jasniewski, Anna J. Komor, John D. Lipscomb, Lawrence Que
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2017)
Article
Chemistry, Multidisciplinary
Williamson N. Oloo, Rahul Banerjee, John D. Lipscomb, Lawrence Que
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2017)
Review
Biochemistry & Molecular Biology
Anna J. Komor, Andrew J. Jasniewski, Lawrence Que, John D. Lipscomb
NATURAL PRODUCT REPORTS
(2018)
Article
Chemistry, Multidisciplinary
George E. Cutsail, Rahul Banerjee, Ang Zhou, Lawrence Que, John D. Lipscomb, Serena DeBeer
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2018)
Article
Biochemistry & Molecular Biology
Melanie S. Rogers, John D. Lipscomb
Article
Biochemistry & Molecular Biology
Jason C. Jones, Rahul Banerjee, Ke Shi, Hideki Aihara, John D. Lipscomb
Article
Biochemistry & Molecular Biology
Delshanee Kotandeniya, Melanie S. Rogers, Jenna Fernandez, Sreenivas Kanugula, Robert H. E. Hudson, Freddys Rodriguez, John D. Lipscomb, Natalia Tretyakova
Summary: Cellular exposure to tobacco-specific nitrosamines leads to the formation of promutagenic DNA adducts, which can be directly repaired by a specific enzyme. By using a highly fluorescent probe, researchers have observed differences in nucleotide flipping rates during DNA repair interactions with AGT.
Review
Chemistry, Multidisciplinary
Rahul Banerjee, John D. Lipscomb
Summary: Rigorous substrate selectivity in enzyme catalysis is attributed to the favorable process of substrate binding to the enzyme active site based on complementary physiochemical characteristics. However, this selectivity becomes more difficult to rationalize for diminutive molecules with too narrow a range of physical characteristics.
ACCOUNTS OF CHEMICAL RESEARCH
(2021)
Article
Biochemistry & Molecular Biology
Jason C. Jones, Rahul Banerjee, Ke Shi, Manny M. Semonis, Hideki Aihara, William C. K. Pomerantz, John D. Lipscomb
Summary: This study investigates the interactions between MMOR and MMOB with sMMOH by specific modifications and F-19 NMR technology. The findings suggest a new regulatory model for the methane conversion cycle, where MMOR and MMOB competitively bind to sMMOH with similar affinity, allowing the transient formation of reactive complexes to advance the reaction cycle.
Article
Biochemistry & Molecular Biology
Jason C. Jones, Rahul Banerjee, Manny M. Semonis, Ke Shi, Hideki Aihara, John D. Lipscomb
Summary: The activity of soluble methane monooxygenase (sMMO) relies on the formation of a complex between the regulatory protein MMOB and the (alpha beta gamma)(2) hydroxylase alpha subunit. Mutations in MMOB can dramatically impact the rate constants for steps in the sMMOH reaction cycle, as revealed in X-ray crystal structures of sMMOH complexes with various variants of MMOB. Different variants alter the formation rate of reaction cycle intermediates and the position of key residues, ultimately affecting sMMO catalysis efficiency.
Article
Biochemistry & Molecular Biology
Melanie S. Rogers, Adrian M. Gordon, Todd M. Rappe, Jason D. Goodpaster, John D. Lipscomb
Summary: This study found that both hydroxylation and methyl hydroxylation of salicylate are catalyzed by monooxygenase chemistry. The functional unit involved in these reactions consists of a nonheme Fe(II) site and a Riesketype iron-sulfur cluster. Fluorine ring substituents were found to decrease the rate of Rieske electron transfer, suggesting a reaction between an Fe(III)-superoxo intermediate and the substrate. It was also discovered that both aromatic and aryl-methyl hydroxylation reactions start with the reaction of Fe(III)-superoxo with a ring carbon, but the latter must be reversible to yield a normal product isotope effect.
Article
Biochemistry & Molecular Biology
Alexander Strom, Rachit Shah, Rafal Dolot, Melanie S. Rogers, Cher-Ling Tong, David Wang, Youlin Xia, John D. Lipscomb, Carston R. Wagner
Summary: Human histidine triad nucleotide-binding proteins play important roles in the activation of antiviral proTides. Different subtypes of these proteins have different functions. Our study reveals that changes in surface residues can affect the function of the proteins.
Article
Biochemistry & Molecular Biology
Anna J. Komor, Brent S. Rivard, Ruixi Fan, Yisong Guo, Lawrence Que, John D. Lipscomb