Abstract
Dr. Katsuko Kakinuma made many important contributions to biology and medicine through the study of the neutrophil NADPH oxidase system, particularly in the investigation of how redox centers transfer an electron to oxygen. In the late 1970s, she moved to the Tokyo Metropolitan Institute of Medical Sciences, where she started her own research as the director in the Department of Inflammation Research. Her special interest was in identifying and observing the key players that are able to pass an electron to oxygen, followed by the generation of superoxide anions by the neutrophil NADPH oxidase system. She started her contributions by solving the “NADPH vs NADH controversy”, identifying the native substrate for the superoxide-generating oxidase in neutrophils. Subsequently, she examined the roles of the flavin molecule, FAD, and the heme of cytochrome b558 in the NADPH oxidase system using spectroscopic methods, performing a detailed analysis of the electron flow from NADPH to oxygen through these redox centers. This chapter describes how these studies were achieved by her research team.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Sbarra AJ, Karnovsky ML (1959) The biochemical basis of phagocytosis. I. Metabolic changes during the ingestion of particles by polymorphonuclear leukocytes. J Biol Chem 234:1355–1362
Rossi F, Zatti M (1964) Changes in the metabolic pattern of polymorphonuclear leukocytes during phagocytosis. Br J Exp Pathol 45:548–559
Romeo D, Cramer R, Rossi F (1970) Use of 1-anilino-8-naphtalene sulfonate to study structural transitions in cell membrane of PMN leucocytes. Biochem Biophys Res Commun 41:582–588
Kakinuma K (1974) Effects of fatty acids on the oxidative metabolism of leukocytes. Biochim Biophys Acta 348:76–85
Kakinuma K, Minakami S (1978) Effects of fatty acids on superoxide radical generation in leukocytes. Biochim Biophys Acta 538:50–59
Kakinuma K, Kaneda M (1980) Kinetic studies on the H2O2 (O2−)-forming enzyme in Guinea pig leukocytes. FEBS Lett 111:90–94
Gabig TG, Babior BM (1979) The O2−-forming oxidase responsible for the respiratory burst in human neutrophils. Properties of the solubilized enzyme. J Biol Chem 254:9070–9074
Light DR, Walsh C, O’Callaghan AM et al (1981) Characteristics of the cofactor requirements for the superoxide-generating NADPH oxidase of human polymorphonuclear leukocytes. Biochemistry 20:1468–1476
Kakinuma K, Fukuhara Y, Kaneda M (1987) The respiratory burst oxidase of neutrophils. Separation of an FAD enzyme and its characterization. J Biol Chem 262:12316–12322
Kakinuma K, Kaneda M, Chiba T, Ohnishi T (1986) Electron spin resonance studies on a flavoprotein in neutrophil plasma membranes: redox potentials of the flavin and its participation in NADPH oxidase. J Biol Chem 261:9426–9432
Vignais PV (2002) The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Cell Mol Life Sci 59:1428–1459
Segal AW, Jones OT (1978) Novel cytochrome b system in phagocytic acuoles of human granulocytes. Nature 276:515–517
Cross AR, Jones OT, Harper AM, Segal AW (1981) Oxidation-reduction properties of the cytochrome b found in the plasma-membrane fraction of human neutrophils. A possible oxidase in the respiratory burst. Biochem J 194:599–606
Hurst JK, Loehr TM, Curnutte JT, Rosen H (1991) Resonance Raman and electron paramagnetic resonance structural investigations of neutrophil cytochrome b558. J Biol Chem 266:1627–1634
Ueno I, Fujii S, Ohya-Nishiguchi H et al (1991) Characterization of neutrophil b-type cytochrome in situ by electron paramagnetic resonance spectroscopy. FEBS Lett 281:130–132
Miki T, Fujii H, Kakinuma K (1992) EPR signals of cytochrome b558 purified from porcine neutrophils. J Biol Chem 267:19673–19675
Fujii H, Johnson MK, Finnegan MG et al (1995) Electron spin resonance studies on neutrophil cytochrome b558: evidence that low-spin heme iron is essential for O2−-generating activity. J Biol Chem 270:12685–12689
Fujii H, Kakinuma K (1992) Electron paramagnetic resonance studies on cytochrome b-558 and peroxidases of pig blood granulocytes. Biochim Biophys Acta 1136:239–246
Yamaguchi T, Hayakawa T, Kaneda M et al (1989) Purification and some properties of the small subuni of cytochrome b558 from human neutrophils. J Biol Chem 264:112–118
Fujii H, Finnegan MG, Miki T et al (1995) Spectroscopic identification of the heme axial ligation of cytochrome b558 in the NADPH oxidase of porcine neutrophils. FEBS Lett 377:345–348
Fujii H, Kakinuma K (1991) Electron transfer reactions in the NADPH oxidase system of neutrophils – involvement of an NADPH-cytochrome c reductase in the oxidase system. Biochim Biophys Acta 1095:201–209
Fujii H, Finnegan MG, Johnson MK (1999) The active form of the ferric heme in neutrophil cytochrome b558 is low-spin in the reconstituted cell-free system in the presence of amphophil. J Biochem 126:708–714
Volpp BD, Nauseef WM, Donelson JE et al (1989) Cloning of the cDNA and functional expression of the 47-kilodalton cytosolic component of human neutrophil respiratory burst oxidase. Proc Natl Acad Sci USA 86:7195–7199
Kaneda M, Sakuraba H, Ohtake A et al (1999) Missense mutations in the gp91-phox gene encoding cytochrome b558 in patients with cytochrome b positive and negative X-linked chronic granulomatous disease. Blood 93:2098–2104
Acknowledgments
All members of the Department of Inflammation Research at the Tokyo Metropolitan Institute of Medical Sciences, who were active at the time that Dr. Kakinuma was the director, thank all the researchers who visited the laboratory, for their valuable and enthusiastic discussions and collaborations. The authors thank Dr. Akio Tomoda, Department of Biochemistry, Tokyo Medical University, for reading this manuscript and for his helpful suggestions.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2023 The Author(s), under exclusive license to Springer Nature Switzerland AG
About this chapter
Cite this chapter
Fujii, H.G., Yoshida, L.S. (2023). On Katsuko Kakinuma: Spectroscopic Studies of Redox Centers in NADPH Oxidase – “Identifying and Observing the Key Players that Pass an Electron to Oxygen”. In: Pick, E. (eds) NADPH Oxidases Revisited: From Function to Structure. Springer, Cham. https://doi.org/10.1007/978-3-031-23752-2_6
Download citation
DOI: https://doi.org/10.1007/978-3-031-23752-2_6
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-031-23751-5
Online ISBN: 978-3-031-23752-2
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)