Journal of Food Science · 1977 · 67 citations · 94 references
ABSTRACT The basis of color in hemè‐pigmented muscle food of mammalian, avian and marine origin resides in the physiocochemical/electromagnetic properties of the oxygen‐carrying heme protein, myoglobin. This paper is a discussion of literature pertaining to the underlying nature and properties of myoglobin and its derivatives that are responsible for the color of fresh, cured and cooked‘red’meat. Factors governing fresh and cured meat color stability and the nature and causes of undesirable changes are also explored. In doing so an attempt is made to interrelate structure, including electronic, with properties.
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Dynamics of ligand binding to myoglobin
Robert H. Austin, K. W. Beeson, L. Eisenstein et al. · Biochemistry · 1975 · 1.6K citations
Richard E. Dickerson, Tsunehiro Takano, David Eisenberg et al. · Journal of Biological Chemistry · 1971 · 878 citations · Full text
G. N. Schrauzer · Bioinorganic Chemistry · 1974 · 831 citations
Nature of the Iron–Oxygen Bond in Oxyhæmoglobin
Nature · 1964 · 412 citations