Results 11 to 20 of about 22,661 (298)

EPR of Co(II) as a Structural and Mechanistic Probe of Metalloprotein Active Sites: A Review of Studies on Aminopeptidase [PDF]

, 2002
Co(II) can often be substituted for Zn(II) in zinc-dependent metalloenzymes to provide spectroscopically accessible forms of the enzymes. Co(II) is an excellent spectroscopic probe as it is both optically active and EPR active.
Bennett, Brian
core   +3 more sources

Computational design of a homotrimeric metalloprotein with a trisbipyridyl core [PDF]

Proceedings of the National Academy of Sciences of the United States of America, 2016
Jeremy H. Mills, William Sheffler, Maraia E. Ener, Patrick J. Almhjell, Gustav Oberdorfer, J.H. Pereira, Fabio Parmeggiani, Banumathi Sankaran, Peter H. Zwart, David Baker   +9 more
openalex   +2 more sources

MetalProGNet: a structure-based deep graph model for metalloprotein–ligand interaction predictions

Chemical Science, 2023
Metalloproteins play indispensable roles in various biological processes ranging from reaction catalysis to free radical scavenging, and they are also pertinent to numerous pathologies including cancer, HIV infection, neurodegeneration, and inflammation.
Dejun Jiang, Zhaofeng Ye, Chang-Yu Hsieh, Zhiyi Yang, Xujun Zhang, Yu Kang, Hongyan Du, Zhenxing Wu, Jike Wang, Yundian Zeng, Haotian Zhang, Xiaorui Wang, Mingyang Wang, Xiaojun Yao, Shengyu Zhang, Jian Wu, Tingjun Hou   +16 more
semanticscholar   +1 more source

Investigation of the Ferredoxin’s Influence on the Anaerobic and Aerobic, Enzymatic H2 Production

Frontiers in Bioengineering and Biotechnology, 2021
Ferredoxins are metalloproteins that deliver electrons to several redox partners, including [FeFe] hydrogenases that are potentially a component of biological H2 production technologies.
Jamin Koo, Yeeun Cha
doaj   +1 more source

Regulating the Coordination Environment of Mesopore‐Confined Single Atoms from Metalloprotein‐MOFs for Highly Efficient Biocatalysis

Advances in Materials, 2022
Single‐atom catalysts (SACs) exhibit unparalleled atomic utilization and catalytic efficiency, yet it is challenging to modulate SACs with highly dispersed single‐atoms, mesopores, and well‐regulated coordination environment simultaneously and ultimately
Jieying Liang, B. Johannessen, Zhibin Wu, R. Webster, Joel Yong, M. Y. Zulkifli, Joshua S. Harbort, You Rou Cheok, Haotian Wen, Z. Ao, Biao Kong, S. Chang, J. Scott, K. Liang   +13 more
semanticscholar   +1 more source

Copper Cytotoxicity: Cellular Casualties of Noncognate Coordination Chemistry

mBio, 2022
Copper (Cu) is an essential micronutrient for cells, but in excess it is cytotoxic. How Cu is cytotoxic is the subject of recent work by L. Zuily, N.
Charlotte I. Z. O’Hern, Karrera Y. Djoko   +1 more
doaj   +1 more source

Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli

Nature Communications, 2022
New cryo-EM structures of the formate hydrogenlyase complex from the model bacterium E. coli clarify how electrons and protons move through the complex and are combined to make H2 gas.
Ralf Steinhilper, Gabriele Höff, Johann Heider, Bonnie J. Murphy   +3 more
doaj   +1 more source

Combinatorial targeting of G‐protein‐coupled bile acid receptor 1 and cysteinyl leukotriene receptor 1 reveals a mechanistic role for bile acids and leukotrienes in drug‐induced liver injury

Hepatology, EarlyView., 2022
CHIN117 is a dual cysteinyl leukotriene receptor 1 (CYSLTR1) antagonist and G‐protein‐coupled bile acid receptor 1 (GPBAR1) agonist. In the liver, GPBAR1 and CYSLTR1 are coexpressed by liver sinusoidal endothelial cells (LSECs), HSCs, circulating monocytes/macrophages, and liver resident macrophages (Kupffer cells).
Michele Biagioli, Silvia Marchianò, Cristina di Giorgio, Rosalinda Roselli, Martina Bordoni, Rachele Bellini, Bianca Fiorillo, Valentina Sepe, Bruno Catalanotti, Chiara Cassiano, Maria Chiara Monti, Eleonora Distrutti, Angela Zampella, Stefano Fiorucci   +13 more
wiley   +1 more source

Engineering a Conformationally Switchable Artificial Metalloprotein.

Journal of the American Chemical Society, 2022
Many naturally occurring metalloenzymes are gated by rate-limiting conformational changes, and there exists a critical interplay between macroscopic structural rearrangements of the protein and subatomic changes affecting the electronic structure of ...
Saman Fatima, D. Boggs, N. Ali, Peter J Thompson, M. Thielges, J. Bridwell-Rabb, Lisa Olshansky   +6 more
semanticscholar   +1 more source

A high-resolution view of the coordination environment in a paramagnetic metalloprotein from its magnetic properties.

Angewandte Chemie, 2021
Metalloproteins constitute a significant fraction of the proteome of all organisms and their characterization is critical for both basic sciences and biomedical applications.
E. Ravera, L. Gigli, E. Suturina, V. Calderone, M. Fragai, G. Parigi, C. Luchinat   +6 more
semanticscholar   +1 more source