Ontology highlight
ABSTRACT:
SUBMITTER: Ross MO
PROVIDER: S-EPMC6953997 | biostudies-literature | 2019 Mar
REPOSITORIES: biostudies-literature
Ross Matthew O MO Fisher Oriana S OS Morgada Marcos N MN Krzyaniak Matthew D MD Wasielewski Michael R MR Vila Alejandro J AJ Hoffman Brian M BM Rosenzweig Amy C AC
Journal of the American Chemical Society 20190307 11
PmoD, a recently discovered protein from methane-oxidizing bacteria, forms a homodimer with a dicopper Cu<sub>A</sub> center at the dimer interface. Although the optical and electron paramagnetic resonance (EPR) spectroscopic signatures of the PmoD Cu<sub>A</sub> bear similarities to those of canonical Cu<sub>A</sub> sites, there are also some puzzling differences. Here we have characterized the rapid formation (seconds) and slow decay (hours) of this homodimeric Cu<sub>A</sub> site to two monon ...[more]