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(white pitcure) 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. ACHMMOBMMOHW308-TunnelDiiron clusterPDB:6YDIThis is the structure of the active site of soluble methanemonooxygenase, an enzyme that catalyzes the redox reaction thattransforms CH4 and O₂ to CH3OH and H₂O. This reaction allowsmethanotrophic organisms to use methanol as fuel. The redox isaccomplished at a diiron cluster, which, in the ferrous (+2) state, isable to reduce O₂ to form a highly oxidized diiron(IV) (+4) speciestermed Q. Q is a strong oxidizing agent able generate methanol byoxidizing methane. The diiron cluster has no inherent specificitythat would allow is to react only with CH4 and O₂ but the enzymestructure around the cluster shown here helps to explain theselectivity of the enzyme. There is a channel shown in blue linedwith hydrophobic amino acids leading to the active diiron. Thehydrophobic nature facilitates passage of non-polar molecules likeCH4 and O₂. Structural changes in the MMOB and MMOHproteins during the reaction cycle constrict the channel at thedashed box so that only O₂ can pass through when the diiron is inthe reducing +2 state and methane when it is in the +4 state. Thisselectivity is key for the organism to effectively use methane asfuel. 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.]

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

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(white pitcure) 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.

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(white pitcure) 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.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 13P

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