Identification and characterisation of the Volvox carteri Moco carrier protein. Issue 11 (24th November 2020)

• Record Type: Journal Article
• Authors: Hercher, Thomas W.; Krausze, Joern; Yang, Jing; Kirk, Martin L.; Kruse, Tobias
• Is Part Of: Bioscience reports. Volume 40:Issue 11(2020)
• Publication Date: 2020-11-24
• Subjects: Molybdenum cofactor -- prosthetic group insertion -- prosthetic group transfer; Molecular biology -- Periodicals; Cytology -- Periodicals; 572.8
• DOI: 10.1042/BSR20202351
• Languages: English
• ISSNs: 0144-8463

Abstract

Abstract: The molybdenum cofactor (Moco) is a redox active prosthetic group found in the active site of Moco-dependent enzymes (Mo-enzymes). As Moco and its intermediates are highly sensitive towards oxidative damage, these are believed to be permanently protein bound during synthesis and upon maturation. As a major component of the plant Moco transfer and storage system, proteins have been identified that are capable of Moco binding and release but do not possess Moco-dependent enzymatic activities. The first protein found to possess these properties was the Moco carrier protein (MCP) from the green alga Chlamydomonas reinhardtii . Here, we describe the identification and biochemical characterisation of the Volvox carteri ( V. carteri ) MCP and, for the first time, employ a comparative analysis to elucidate the principles behind MCP Moco binding. Doing so identified a sequence region of low homology amongst the existing MCPs, which we showed to be essential for Moco binding to V. carteri MCP.