1993Chemistry LettersRequires access

Binding of Heme to Sperm Whale Myoglobin-(57–96)-Tetracontapeptide

Chikao Hashimoto, Ichiro Muramatsu

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Abstract

Abstract The binding of heme to sperm whale myoglobin-(57–96)-tetracontapeptide (1) was investigated. The appearance of a peak at 414 nm in the difference spectrum between a 1–heme mixture and heme indicated the formation of a complex. The circular dichroism spectrum of the mixture showed that an α-helical structure is induced and stabilized by the formation of the complex.

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Abstract The binding of heme to sperm whale myoglobin-(57–96)-tetracontapeptide (1) was investigated. The appearance of a peak at 414 nm in the difference spectrum between a 1–heme mixture and heme indicated the formation of a complex. The circular dichroism spectrum of the mixture showed that an α-helical structure is induced and stabilized by the formation of the complex.

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Available abstract

Abstract The binding of heme to sperm whale myoglobin-(57–96)-tetracontapeptide (1) was investigated. The appearance of a peak at 414 nm in the difference spectrum between a 1–heme mixture and heme indicated the formation of a complex. The circular dichroism spectrum of the mixture showed that an α-helical structure is induced and stabilized by the formation of the complex.

Key concepts: Chemistry, Myoglobin, Sperm whale, Heme, Whale, Hemeprotein, Zoology, Fishery

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