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J Biol Chem, Vol. 273, Issue 43, 27879-27886, October 23, 1998

Mutation at Histidine 338 of gp91phox Depletes FAD and Affects Expression of Cytochrome b558 of the Human NADPH Oxidase

Lucia S. Yoshida, Fumiko Saruta, Ken Yoshikawa, Osamu Tatsuzawa, and Shohko Tsunawaki

From the National Children's Medical Research Center, Setagaya-ku, Tokyo, 154-8509, Japan

Defective NADPH oxidase components prevent superoxide (Obardot 2) generation, causing chronic granulomatous disease (CGD). X-linked CGD patients have mutations in the gene encoding the gp91phox subunit of cytochrome b558 and usually lack gp91phox protein completely (X910). gp91phox is considered to be a flavocytochrome that contains binding sites for NADPH, FAD, as well as heme. We here report a rare X-linked CGD patient whose neutrophils entirely failed to produce Obardot 2, but presented a diminished expression of gp91phox containing about one-third of the heme present in normal individuals by Soret absorption. Translocation of cytosolic factors p67phox and p47phox was normal. However, the FAD content in his neutrophil membranes was as low as that of X910 patients, suggesting complete depletion of FAD in his gp91phox. This was in agreement with the finding that a single base substitution (C1024 to T) changed His-338 to Tyr in gp91phox in a predicted FAD-binding domain of the flavocytochrome model. The loss of FAD could not be corrected even after addition of reagent FAD or a FAD-rich dehydrogenase fraction isolated from normal neutrophils to the patient's membranes, in a reconstitution in vitro with normal cytosol. These results indicate that His-338 is a very critical residue for FAD incorporation into the NADPH oxidase system. This is the first such mutation found in CGD.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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