Electron transfer properties of the soluble Cyt-domain from Rhodothermus

MOLINAS, MARÍA FLORENCIA; CAPDEVILA, DAIANA; DE CANDIA, ARIEL; RODRIGUEZ, JUAN BAUTISTA; TODOROVIC, SMILJA; MARTÍ, MARCELO A.; MURGIDA, DANIEL H.

Salta, Argentina

Congreso; 3rd Latin American Protein Society Meeting; 2010

Latin American Protein Society

Heme/copper oxygen reductases (ORs) constitute a superfamily of membrane-bound enzymes that catalyse the reduction of dioxygen to water as a terminal step in the respiratory chains of aerobic organisms. Rhodothermus marinus is an aerobic thermohalophilic bacteria whose terminal enzymatic complex of aerobic respiratory chain contain a CuA centre and a c-type heme in the C-terminal region of its subunit II (Rm ccd) wich can be expressed separately yielding a soluble stable protein domain. Its putative partner is a high potential iron-sulfur protein (HiPIP) wich is a small protein with a Fe-S cluster. We studied the electron transfer (ET) properties of Rm ccd and HiPIP using surface enhanced resonance Raman (SERR), time resolved SERR (TR-SERR), cyclic voltammetry (CV) and molecular dynamics simulations (MD)