Spectroscopic characterization of a green copper site in a single-domain cupredoxin.

ABSTRACT: Cupredoxins are widespread copper-binding proteins, mainly involved in electron transfer pathways. They display a typical rigid greek key motif consisting of an eight stranded β-sandwich. A fascinating feature of cupredoxins is the natural diversity of their copper center geometry. These geometry variations give rise to drastic changes in their color, such as blue, green, red or purple. Based on several spectroscopic and structural analyses, a connection between the geometry of their copper-binding site and their color has been proposed. However, little is known about the relationship between such diversity of copper center geometry in cupredoxins and possible implications for function. This has been difficult to assess, as only a few naturally occurring green and red copper sites have bee

SUBMITTER: Roger M 

PROVIDER: S-EPMC4059628 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature