@inbook{7f20a2aaec5a4925b79425a1e7546df8,
title = "Metal reconstitution of particulate methane Monooxygenase and heterologous expression of the pmoB subunit",
abstract = "Particulate methane monooxygenase (pMMO) is a multisubunit metalloenzyme complex used by methanotrophic bacteria to oxidize methane in the first step of carbon assimilation and energy production. In this chapter, we detail methods to prepare metal free (apo) membrane-bound pMMO and to reconstitute apo pMMO with metal ions. We also describe protocols to clone, express, and refold metal-loaded soluble domain constructs of the pmoB subunit. These approaches were used to address fundamental questions concerning the metal content and location of the pMMO active site.",
author = "Smith, {Stephen M.} and Ramakrishnan Balasubramanian and Rosenzweig, {Amy C.}",
note = "Funding Information: This work was supported by NIH grant GM070473. We thank Liliya Yatsunyk, Megen Culpepper, Swati Rawat, and Timothy Stemmler for assistance at various stages of this project.",
year = "2011",
doi = "10.1016/B978-0-12-386905-0.00013-9",
language = "English (US)",
series = "Methods in Enzymology",
publisher = "Academic Press Inc",
pages = "195--210",
booktitle = "Methods in Enzymology",
}