Human ferredoxin-2 displays a unique conformational change

Abstract

Human ferredoxin-1 (hFd1) and human ferredoxin-2 (hFd2) share high sequence similarity but serve on distinct cellular pathways. A unique conformational change is observed when holo hFd2 is warmed to physiological temperatures, or higher. Enzymatic studies show that this conformational change causes the increase of affinity between hFd2 and adrenodoxin reductase. No such change was observed for hFd1, which may contribute to the distinct cellular functions of hFd1 and hFd2 under physiological conditions.