Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane

By R. Lieberman, A. Rosenzweig. Nature, 2005

598 citations recorded by the source corpus.

Subfields: Inorganic Chemistry, Molecular Biology, Renewable Energy, Sustainability and the Environment

View Paper: https://www.semanticscholar.org/paper/c09557ecc66c60e4c6c4c651f2d8055779a9c820

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In Inorganic Chemistry

In Molecular Biology

In Renewable Energy, Sustainability and the Environment

Citations in the corpus

7 Aerobic Methylotrophic Prokaryotes (2013, background): “Crystal structures of pMMO enzymes from different bacteria have also been determined (Lieberman and Rosenzweig 2005; Hakemian et al. 2008), and the role of a dicopper center in the catalysis has been unequivocally proven (Balasubramanian et al.”
Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea (2010, background): “Notably, mapping the sequence encoded by amoB onto the pmoB crystal structure of Methylococcus capsulatus (Bath) (28) reveals the conservation of the ligands to the pMMO metal centers and the complete absence of both a transmembrane helix and a C-terminal cupredoxin domain predicted to be present in”
Alkane hydroxylases involved in microbial alkane degradation (2007, background): “However, recent work by two independent groups has now revealed the structure of the elusive pMMO (Kitmitto et al. 2005; Lieberman and Rosenzweig 2005).”
Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components (2011, background): “) Intriguingly, the closest structural match was found with the putative active site of copper methane mono-oxygenase (CuMMO),where the histidine bracewas also observed (21, 22), albeit at a coordination site that, informed by extendedX-ray absorption fine structure and EPR studies, was modeled with”
Methanotrophs and copper. (2010, methodology): “Membrane orientation was predicted using the methodology of Lomize et al. (2006) using structural information from Lieberman & Rosenzweig (2005) and Hakemian et al. (2008).”
Single-site trinuclear copper oxygen clusters in mordenite for selective conversion of methane to methanol (2015, unknown): “A supercell of all-silica MOR, constructed by a doubling monoclinic primitive cell along the c axis with lattice parameters of a ¼ b ¼ 13.648, c ¼ 15.015Å and g ¼ 97.2 (cid:2) as optimized by DFT, was used as an initial model 47 .”
Novel genes for nitrite reductase and Amo-related proteins indicate a role of uncultivated mesophilic crenarchaeota in nitrogen cycling. (2005, background): “Arrows point to amino acids predicted in metal coordination in Pmo of Methylococcus capsulatus Bath ( Lieberman and Rosenzweig, 2005 ); filled arrow: dinuclear copper centre (conserved throughout bacterial and archaeal proteins); open arrows: mononuclear centre (less/not conserved throughout the pro”
How do bacterial cells ensure that metalloproteins get the correct metal? (2009, background): “This is exemplified by the replacement of iron-requiring, soluble methane monooxygenase with the copper-requiring particulate enzyme in methanotrophic bacteri”