The structure of a metalloenzyme active site is down below(black picture). Describe, from a chemical and structural perspective, how the reactive site is designed to facilitate its catalytic reaction. The example below suggests the level of detail that is required. Make sure that you explain what the metal is doing, what the reaction is, and its biological significance. AB172spmoB265spmoBd2spmoBd1See this image and copyright information in PMCFigure 1 Overall architecture of pMMO. (A) Structure of Methylocystis sp. strain M pMMOprotomer (PDB accession code 3RGR). The pmoB, pmoA, and pmoC subunits are shown inblue, magenta, and green, respectively. The N- and C-termini of pmoB are labeled. Anexogenous helix is shown in yellow. Copper ions are shown as cyan spheres and a zinc ion isshown as a gray sphere. Ligands are shown as ball-and-stick representations. (B) Structure ofM. capsulatus (Bath) pMMO protomer (PDB accession code 3RGB). The amino terminaldomain of pmoB (spmoBd1) is shown in blue, the carboxy terminal domain of pmoB is shownin gray (spmoBd2), and the two transmembrane helices are shown in transparent blue. In therecombinant spmoB protein, spmoBd1 and spmoBd2 are linked by a GKLGGG sequenceconnecting residues 172 and 265 (labeled). The pmoA and pmoC subunits are shown intransparent magenta and transparent green, respectively. A hydrophilic patch of residuesproposed to house a tricopper active site is denoted with an asterisk. The mononuclearcopper site at the interface of the two spmoB domains is not present in the Methylocystis sp.strain M pMMO structure. [A color version of this figure is available online.] Architecture and active site of particulate methanemonooxygenaseMegen A Culpepper 1, Amy C RosenzweigAffiliations expandPMID: 22725967 PMCID: PMC3474877 DOI: 10.3109/10409238.2012.697865Free PMC articleAbstractParticulate methane monooxygenase (pMMO) is an integral membrane metalloenzyme thatoxidizes methane to methanol in methanotrophic bacteria, organisms that live on methane gas astheir sole carbon source. Understanding pMMO function has important implications forbioremediation applications and for the development of new, environmentally friendly catalysts forthe direct conversion of methane to methanol. Crystal structures of pMMOs from three differentmethanotrophs reveal a trimeric architecture, consisting of three copies each of the pmoB, pmoA,and pmoC subunits. There are three distinct metal centers in each protomer of the trimer,mononuclear and dinuclear copper sites in the periplasmic regions of pmoB and a mononuclear sitewithin the membrane that can be occupied by copper or zinc. Various models for the pMMO activesite have been proposed within these structural constraints, including dicopper, tricopper, anddiiron centers. Biochemical and spectroscopic data on pMMO and recombinant soluble fragments,denoted spmoB proteins, indicate that the active site involves copper and is located at the site ofthe dicopper center in the pmoB subunit. Initial spectroscopic evidence for O(2) binding at this sitehas been obtained. Despite these findings, questions remain about the active site identity andnuclearity and will be the focus of future studies.FiguresFigure 1 Overallarchitecture of pMMO.(A)...MMOпропTOFigure 4 Opticalspectrum of detergent-solubilized pMMO...न्छु ९०द्र प्रबुद्ध3337Figure 2 Metal centersmodeled in the...Figure 3 Multiplesequence alignments ofrepresentative...

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Methane monooxygenase (MMO) is present in methanotrophic bacteria and MMO is present in an integral…