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On the geometry of leukocyte NADPH‐oxidase, a membrane flavoenzyme
Author(s) -
Schirmer R.Heiner,
Schulz Georg E.,
Untucht-Grau Renate
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80865-5
Subject(s) - nadph oxidase , glutathione reductase , flavin group , chemistry , glutathione , oxidase test , nad+ kinase , reductase , membrane , biophysics , nad(p)h oxidase , biochemistry , redox , stereochemistry , reactive oxygen species , enzyme , biology , glutathione peroxidase , inorganic chemistry
Using the structure of glutathione reductase as a model, we suggest the following topography for leukocyte NADPH‐oxidase: The binding sites of NADPH and O 2 are separated from each other by the flavin ring and are thus exposed to opposite sides of the plasma membrane. This model supports the concept that O − 2 is formed at the membrane facing the extracellular or phagosomal space, respectively. The fate of the proton produced in the reaction NADPH + 2 O 2 → NADP + 2 O − 2 + H + is also discussed in light of our model. NAD(P)H‐oxidases possessing the topography of glutathione reductase may establish transmembrane proton gradients. Consequently our model suggests that leukocyte NADPH‐oxidase produces not only the O − 2 burst but also a proton burst.