Nicolas Grosjean, Estella F Yee, Desigan Kumaran, Kriti Chopra, Macon Abernathy, Sandeep Biswas, James Byrnes, Dale F Kreitler, Jan-Fang Cheng, Agnidipta Ghosh, Steven C Almo, Masakazu Iwai, Krishna K Niyogi, Himadri B Pakrasi, Ritimukta Sarangi, Hubertus van Dam, Lin Yang, Ian K Blaby, Crysten E Blaby-Haas
Heme has a critical role in the chemical framework of the cell as an essential protein cofactor and signaling molecule that controls diverse processes and molecular interactions. Using a phylogenomics-based approach and complementary structural techniques, we identify a family of dimeric hemoproteins comprising a domain of unknown function DUF2470. The heme iron is axially coordinated by two zinc-bound histidine residues, forming a distinct two-fold symmetric zinc-histidine-iron-histidine-zinc site. Together with structure-guided in vitro and in vivo experiments, we further demonstrate the existence of a functional link between heme binding by Dri1 (Domain related to iron 1, formerly ssr1698) and post-translational regulation of succinate dehydrogenase in the cyanobacterium Synechocystis, suggesting an iron-dependent regulatory link between photosynthesis and respiration...
April 12, 2024: Nature Communications