Abstract
Arthropod Hcs are multisubunit proteins (1). The smallest arthropod found in nature consists of six subunits. Each subunit (M r = 75 kDa) is composed of three domains (2). The active site is located in the second domain, where O2 is reversibly bound in a complex bridged between two copper atoms (3). Each copper atom is liganded to side-chain groups of the protein. Little data regarding the thermal stability of Hcs are available (4). This study presents the influence of the intact active site and of the quaternary state on the stability of an arthropod He with respect to temperature change.
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© 1991 Springer-Verlag New York, Inc.
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Penz, F., Decker, H. (1991). Spectroscopic Analysis of Temperature-Induced Unfolding of the Hemocyanin from the Tarantula Eurypelma californicum . In: Vinogradov, S.N., Kapp, O.H. (eds) Structure and Function of Invertebrate Oxygen Carriers. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3174-5_5
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DOI: https://doi.org/10.1007/978-1-4612-3174-5_5
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