NMR Structure of the Flavin Domain from Soluble Methane Monooxygenase Reductase from <i>Methylococcus capsulatus</i> (Bath)<sup>,</sup>

Chatwood, Lisa L.; Müller, Jens; Gross, John D.; Wagner, Gerhard; Lippard, Stephen J.

doi:10.1021/bi049066n

Cited by 44 publications

(44 citation statements)

References 51 publications

(121 reference statements)

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“…Structures of the isolated reduced ferredoxin domain and reduced FAD- and NADH-binding domains have been determined via NMR [50, 51]. Interactions between the ferredoxin and hydroxylase components have been observed crystallographically for the BMM toluene 4-monooxygenase, in which the reduced ferredoxin domain binds in the hydroxylase canyon region atop the pore [52].…”

Section: Soluble Methane Monooxygenasementioning

confidence: 99%

A tale of two methane monooxygenases

Ross¹,

2016

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Methane monooxygenase (MMO) enzymes activate O2 for oxidation of methane. Two distinct MMOs exist in nature, a soluble form that uses a diiron active site (sMMO) and a membrane-bound form with a catalytic copper center (pMMO). Understanding the reaction mechanisms of these enzymes is of fundamental importance to biologists and chemists, and is also relevant to the development of new biocatalysts. The sMMO catalytic cycle has been elucidated in detail, including O2 activation intermediates and the nature of the methane-oxidizing species. By contrast, many aspects of pMMO catalysis remain unclear, most notably the nuclearity and molecular details of the copper active site. Here, we review the current state of knowledge for both enzymes, and consider pMMO O2 activation intermediates suggested by computational and synthetic studies in the context of existing biochemical data. Further work is needed on all fronts, with the ultimate goal of understanding how these two remarkable enzymes catalyze a reaction not readily achieved by any other metalloenzyme or biomimetic compound.

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Section: Soluble Methane Monooxygenasementioning

confidence: 99%

A tale of two methane monooxygenases

Ross¹,

2016

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“…sMMO is encoded by a six-gene operon, mmoXYBZDC, and has three components: (i) a 250-kDa hydroxylase with an ␣ 2 ␤ 2 ␥ 2 structure in which the ␣ subunits (MmoX) contain the binuclear iron active center where substrate oxygenation occurs, (ii) a 39-kDa NAD(P)H-dependent reductase (MmoC) with flavin adenine dinucleotide (FAD) and Fe 2 S 2 prosthetic groups, and (iii) a 16-kDa component (MmoB) known as protein B or coupling/gating protein that does not contain prosthetic groups or metal ions (39,48). There are X-ray crystal structures for the hydroxylase component (49)(50)(51)(52), nuclear magnetic resonance (NMR)-derived structures for protein B (39,53,54), and an NMR-derived structure for the flavin domain of the reductase (55). The complex formed by the three components has been studied structurally via small-angle X-ray scattering analysis and biophysically by electron paramagnetic resonance spectroscopy, ultracentrifugation, and calorimetric analysis (56,57).…”

Section: Physiology and Biochemistry Of Methanotrophsmentioning

confidence: 99%

Methanobactin and the Link between Copper and Bacterial Methane Oxidation

DiSpirito

Semrau

Murrell

et al. 2016

Microbiol Mol Biol Rev

128

157

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SUMMARYMethanobactins (mbs) are low-molecular-mass (<1,200 Da) copper-binding peptides, or chalkophores, produced by many methane-oxidizing bacteria (methanotrophs). These molecules exhibit similarities to certain iron-binding siderophores but are expressed and secreted in response to copper limitation. Structurally, mbs are characterized by a pair of heterocyclic rings with associated thioamide groups that form the copper coordination site. One of the rings is always an oxazolone and the second ring an oxazolone, an imidazolone, or a pyrazinedione moiety. The mb molecule originates from a peptide precursor that undergoes a series of posttranslational modifications, including (i) ring formation, (ii) cleavage of a leader peptide sequence, and (iii) in some cases, addition of a sulfate group. Functionally, mbs represent the extracellular component of a copper acquisition system. Consistent with this role in copper acquisition, mbs have a high affinity for copper ions. Following binding, mbs rapidly reduce Cu2+to Cu1+. In addition to binding copper, mbs will bind most transition metals and near-transition metals and protect the host methanotroph as well as other bacteria from toxic metals. Several other physiological functions have been assigned to mbs, based primarily on their redox and metal-binding properties. In this review, we examine the current state of knowledge of this novel type of metal-binding peptide. We also explore its potential applications, how mbs may alter the bioavailability of multiple metals, and the many roles mbs may play in the physiology of methanotrophs.

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“…MMOR consists of a NAD binding domain, a FAD-binding domain and a ferredoxin ( Fig. 4A) (Chatwood 2004). As can be seen both NAD ( Fig.…”

Section: Methane Monooxygenase Reductase (Mmor)mentioning

confidence: 96%

Evaluating apoenzyme–coenzyme–substrate interactions of methane monooxygenase with an engineered active site for electron harvesting: a computational study

2018

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Energy generation via natural gas is viewed as one of the most promising environmentally friendly solutions for ever-increasing energy demand. Of the several alternatives available, natural gas-powered fuel cells are considered to be one of the most efficient for producing energy. Biocatalysts, present in methanotrophs, known as methane monooxygenases (MMOs) are well known for their ability to quite effectively activate and oxidize methane at lowtemperature. To utilize MMOs effectively in a fuel cell, the enzymes should be directly attached onto the anode. However, there is a knowledge gap on how to attach MMOs to an electrode and once attached the impact of active site modification on enzyme functionality. The overall goal of this work was to computationally evaluate the feasibility of attaching MMOs to a metal electrode and evaluate its functionality using docking and molecular dynamic (MD) simulations. It is surmised that MMOs could be attached to a metal electrode by engineering the active site, i.e., Flavin Adenine Dinucleotide (FAD) coenzyme to attract metal clusters (surfaces) via Fe-S functionalization and such modification will keep the active site functionality unfettered. This work was geared toward performing a structural analysis to identify the spatial distribution of FAD binding site(s) in correlation to Nicotinamide Adenine Dinucleotide (NAD) and subsequently to evaluate the feasibility of utilizing FeS-functionalized FAD for anchoring the enzyme system to a metal electrode. This work is intended to provide valuable mechanistic insights on critical chemical iii reactions that occur within the apoenzyme/coenzyme system and electron transport pathways so that future researchers could utilize the knowledge when fabricating MMO-based electrodes to be used in fuel cells. iv DEDICATION This work is dedicated to my family who are always with me and supporting me from overseas and those who are still under intensive lab work guided by their aspiration of the truth.

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NMR Structure of the Flavin Domain from Soluble Methane Monooxygenase Reductase from Methylococcus capsulatus (Bath)^,

Cited by 44 publications

References 51 publications

A tale of two methane monooxygenases

A tale of two methane monooxygenases

Methanobactin and the Link between Copper and Bacterial Methane Oxidation

Evaluating apoenzyme–coenzyme–substrate interactions of methane monooxygenase with an engineered active site for electron harvesting: a computational study

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NMR Structure of the Flavin Domain from Soluble Methane Monooxygenase Reductase from Methylococcus capsulatus (Bath),

Cited by 44 publications

References 51 publications

A tale of two methane monooxygenases

A tale of two methane monooxygenases

Methanobactin and the Link between Copper and Bacterial Methane Oxidation

Evaluating apoenzyme–coenzyme–substrate interactions of methane monooxygenase with an engineered active site for electron harvesting: a computational study

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Product

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NMR Structure of the Flavin Domain from Soluble Methane Monooxygenase Reductase from Methylococcus capsulatus (Bath)^,