Methanotrophs, also called aerobic methane oxidizing bacteria (AMOB), are a group of bacteria that use methane as their sole source of carbon and energy. AMOB share a general pathway for the metabolism of methane to carbon dioxide. The first step in AMOB metabolism is the oxidation of methane to methanol. The enzyme methane monooxygenase is responsible for the first step in methane metabolism. Methanotrophs have a large demand for copper and have been shown to produce an extracellular copper binding compound (cbc) now termed methanobactin (mb).

Methanobactin is a small, <1200 Da, post-translationally modified protein excreted by bacteria for the purpose of scavenging copper from the environment. To date 5 methanobactins have been structurally characterized. This dissertation examines the binding properties of the structurally unique methanobactin from the facultative methanotroph Methylocystis strain SB2 (mb-SB2). The first part of the dissertation focuses on the isolation procedures for acquiring metal free methanobactin.

The second part of the dissertation presents evidence that less structurally complex forms of methanobactin have similar copper binding properties to previously isolated forms of methanobactin. Mb-SB2 is shown to have transition metal binding properties that areM similar to those found in the complex form of mb from Methylosinus trichosporium OB3b (mb-OB3b). Attention is given to the ability of mb-SB2 to form gold nanoparticles.