Skip to content
TrackPodcasts
healthOct 18, 202136:40pending

PubReading [39] - Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane - R. L. Lieberman and A. C. Rosenzweig

PubReading

About this episode

Particulate methane monooxygenase (pMMO) is an integral membrane metalloenzyme that catalyses the conversion of methane to methanol. Knowledge of how pMMO performs this extremely challenging chemistry may have an impact on the use of methane as an alternative energy source by facilitating the development of new synthetic catalysts. We have determined the structure of pMMO from the methanotroph Methylococcus capsulatus (Bath) to a resolution of 2.8A ̊. The enzyme is a trimer with an a3b3g3 polypeptide arrangement. Two metal centres, modelled as mononuclear copper and dinuclear copper, are located in soluble regions of each pmoB subunit, which resembles cytochrome c oxidase subunit II. A third metal centre, occupied by zinc in the crystal, is located within the membrane. The structure provides new insight into the molecular details of biological methane oxidation. - doi.org/10.1038/nature03311 - 2005

Get every episode summarized

Each time PubReading publishes, we email you a written briefing from the transcript — the topics, who appeared, and any specific claims, with the ad reads skipped.

Email me new episodes

Free for 3 shows. No card needed.

Hosts & guests

No transcript yet

This episode has not been transcribed. Request it and it moves to the front of the queue.

PubReading [39] - Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane - R. L. Lieberman and A. C. Rosenzweig

PubReading

0:00
36:40

More episodes

More from PubReading

View all episodes →