The quest for the particulate methane monooxygenase active site

2005 ◽  
pp. 3390 ◽  
Author(s):  
Raquel L. Lieberman ◽  
Amy C. Rosenzweig
Keyword(s):  
Active Site ◽  
Methane Monooxygenase ◽  
Particulate Methane Monooxygenase

scholarly journals Redox Potentiometry Studies of Particulate Methane Monooxygenase: Support for a Trinuclear Copper Cluster Active Site

2007 ◽  
Vol 119 (12) ◽  
pp. 2038-2040 ◽  
Author(s):  
Sunney I. Chan ◽  
Vincent C.-C. Wang ◽  
Jeff C.-H. Lai ◽  
Steve S.-F. Yu ◽  
Peter P.-Y. Chen ◽  
...  
Keyword(s):  
Active Site ◽  
Methane Monooxygenase ◽  
Copper Cluster ◽  
Particulate Methane Monooxygenase ◽  
Redox Potentiometry

scholarly journals Redox Potentiometry Studies of Particulate Methane Monooxygenase: Support for a Trinuclear Copper Cluster Active Site

2007 ◽  
Vol 46 (12) ◽  
pp. 1992-1994 ◽  
Author(s):  
Sunney I. Chan ◽  
Vincent C.-C. Wang ◽  
Jeff C.-H. Lai ◽  
Steve S.-F. Yu ◽  
Peter P.-Y. Chen ◽  
...  
Keyword(s):  
Active Site ◽  
Methane Monooxygenase ◽  
Copper Cluster ◽  
Particulate Methane Monooxygenase ◽  
Redox Potentiometry

scholarly journals Particulate methane monooxygenase contains only mononuclear copper centers

Science ◽  
2019 ◽  
Vol 364 (6440) ◽  
pp. 566-570 ◽  
Author(s):  
Matthew O. Ross ◽  
Fraser MacMillan ◽  
Jingzhou Wang ◽  
Alex Nisthal ◽  
Thomas J. Lawton ◽  
...  
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Methane Oxidation ◽  
Active Site ◽  
Methane Monooxygenase ◽  
Spectroscopic Characterization ◽  
Metabolic Enzyme ◽  
Particulate Methane Monooxygenase ◽  
Paramagnetic Resonance ◽  
Membrane Bound ◽  
Electron Paramagnetic

Bacteria that oxidize methane to methanol are central to mitigating emissions of methane, a potent greenhouse gas. The nature of the copper active site in the primary metabolic enzyme of these bacteria, particulate methane monooxygenase (pMMO), has been controversial owing to seemingly contradictory biochemical, spectroscopic, and crystallographic results. We present biochemical and electron paramagnetic resonance spectroscopic characterization most consistent with two monocopper sites within pMMO: one in the soluble PmoB subunit at the previously assigned active site (CuB) and one ~2 nanometers away in the membrane-bound PmoC subunit (CuC). On the basis of these results, we propose that a monocopper site is able to catalyze methane oxidation in pMMO.

scholarly journals Evidence for Oxygen Binding at the Active Site of Particulate Methane Monooxygenase

2012 ◽  
Vol 134 (18) ◽  
pp. 7640-7643 ◽  
Author(s):  
Megen A. Culpepper ◽  
George E. Cutsail ◽  
Brian M. Hoffman ◽  
Amy C. Rosenzweig
Keyword(s):  
Active Site ◽  
Methane Monooxygenase ◽  
Oxygen Binding ◽  
Particulate Methane Monooxygenase

scholarly journals Cerium Regulates Expression of Alternative Methanol Dehydrogenases in Methylosinus trichosporium OB3b

2015 ◽  
Vol 81 (21) ◽  
pp. 7546-7552 ◽  
Author(s):  
Muhammad Farhan Ul Haque ◽  
Bhagyalakshmi Kalidass ◽  
Nathan Bandow ◽  
Erick A. Turpin ◽  
Alan A. DiSpirito ◽  
...  
Keyword(s):  
Active Site ◽  
Methane Monooxygenase ◽  
Particulate Methane Monooxygenase ◽  
Methylosinus Trichosporium Ob3b ◽  
Methylosinus Trichosporium ◽  
Content Type ◽  
Expression Levels ◽  
Soluble Methane Monooxygenase ◽  
Discernible Effect ◽  
Expression And Activity

ABSTRACTMethanotrophs have multiple methane monooxygenases that are well known to be regulated by copper, i.e., a “copper switch.” At low copper/biomass ratios the soluble methane monooxygenase (sMMO) is expressed while expression and activity of the particulate methane monooxygenase (pMMO) increases with increasing availability of copper. In many methanotrophs there are also multiple methanol dehydrogenases (MeDHs), one based on Mxa and another based on Xox. Mxa-MeDH is known to have calcium in its active site, while Xox-MeDHs have been shown to have rare earth elements in their active site. We show here that the expression levels of Mxa-MeDH and Xox-MeDH inMethylosinus trichosporiumOB3b significantly decreased and increased, respectively, when grown in the presence of cerium but the absence of copper compared to the absence of both metals. Expression of sMMO and pMMO was not affected. In the presence of copper, the effect of cerium on gene expression was less significant, i.e., expression of Mxa-MeDH in the presence of copper and cerium was slightly lower than in the presence of copper alone, but Xox-MeDH was again found to increase significantly. As expected, the addition of copper caused sMMO and pMMO expression levels to significantly decrease and increase, respectively, but the simultaneous addition of cerium had no discernible effect on MMO expression. As a result, it appears Mxa-MeDH can be uncoupled from methane oxidation by sMMO inM. trichosporiumOB3b but not from pMMO.

scholarly journals Inhibition of Ammonia Monooxygenase from Ammonia-Oxidizing Archaea by Linear and Aromatic Alkynes

2020 ◽  
Vol 86 (9) ◽  
Author(s):  
Chloë L. Wright ◽  
Arne Schatteman ◽  
Andrew T. Crombie ◽  
J. Colin Murrell ◽  
Laura E. Lehtovirta-Morley
Keyword(s):  
Active Site ◽  
Methane Monooxygenase ◽  
Active Form ◽  
Ammonia Oxidizing Bacteria ◽  
Methylococcus Capsulatus ◽  
Ammonia Monooxygenase ◽  
Particulate Methane Monooxygenase ◽  
Short Chain Length ◽  
Content Type ◽  
Ammonia Oxidizing Archaea

ABSTRACT Ammonia monooxygenase (AMO) is a key nitrogen-transforming enzyme belonging to the same copper-dependent membrane monooxygenase family (CuMMO) as the particulate methane monooxygenase (pMMO). The AMO from ammonia-oxidizing archaea (AOA) is very divergent from both the AMO of ammonia-oxidizing bacteria (AOB) and the pMMO from methanotrophs, and little is known about the structure or substrate range of the archaeal AMO. This study compares inhibition by C2 to C8 linear 1-alkynes of AMO from two phylogenetically distinct strains of AOA, “Candidatus Nitrosocosmicus franklandus” C13 and “Candidatus Nitrosotalea sinensis” Nd2, with AMO from Nitrosomonas europaea and pMMO from Methylococcus capsulatus (Bath). An increased sensitivity of the archaeal AMO to short-chain-length alkynes (≤C5) appeared to be conserved across AOA lineages. Similarities in C2 to C8 alkyne inhibition profiles between AMO from AOA and pMMO from M. capsulatus suggested that the archaeal AMO has a narrower substrate range than N. europaea AMO. Inhibition of AMO from “Ca. Nitrosocosmicus franklandus” and N. europaea by the aromatic alkyne phenylacetylene was also investigated. Kinetic data revealed that the mechanisms by which phenylacetylene inhibits “Ca. Nitrosocosmicus franklandus” and N. europaea are different, indicating differences in the AMO active site between AOA and AOB. Phenylacetylene was found to be a specific and irreversible inhibitor of AMO from “Ca. Nitrosocosmicus franklandus,” and it does not compete with NH3 for binding at the active site. IMPORTANCE Archaeal and bacterial ammonia oxidizers (AOA and AOB, respectively) initiate nitrification by oxidizing ammonia to hydroxylamine, a reaction catalyzed by ammonia monooxygenase (AMO). AMO enzyme is difficult to purify in its active form, and its structure and biochemistry remain largely unexplored. The bacterial AMO and the closely related particulate methane monooxygenase (pMMO) have a broad range of hydrocarbon cooxidation substrates. This study provides insights into the AMO of previously unstudied archaeal genera, by comparing the response of the archaeal AMO, a bacterial AMO, and pMMO to inhibition by linear 1-alkynes and the aromatic alkyne, phenylacetylene. Reduced sensitivity to inhibition by larger alkynes suggests that the archaeal AMO has a narrower hydrocarbon substrate range than the bacterial AMO, as previously reported for other genera of AOA. Phenylacetylene inhibited the archaeal and bacterial AMOs at different thresholds and by different mechanisms of inhibition, highlighting structural differences between the two forms of monooxygenase.

Modelling a ‘histidine brace’ motif in mononuclear copper monooxygenases

2020 ◽  
Vol 56 (38) ◽  
pp. 5123-5126
Author(s):  
Arisa Fukatsu ◽  
Yuma Morimoto ◽  
Hideki Sugimoto ◽  
Shinobu Itoh
Keyword(s):  
Copper Complex ◽  
Active Site ◽  
Methane Monooxygenase ◽  
Particulate Methane Monooxygenase ◽  
Site Model ◽  
Lytic Polysaccharide Monooxygenases ◽  
Active Site Model ◽  
Polysaccharide Monooxygenases

A mononuclear copper complex bearing a ‘histidine brace’ is synthesised and characterised as an active-site model of mononuclear copper monooxygenases such as lytic polysaccharide monooxygenases (LPMOs) and particulate methane monooxygenase (pMMO).

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