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Hemoglobin was incubated with aldehydes such as propionaldehyde, formaldehyde, acetaldehyde, acrolein, crotonaldehyde, trichloroacetic acid, methyl vinyl ketone, methyl methacrylate, acrolein, glutaraldehyde, glycidol and glyoxal. Redox reactions of adducts of hemoglobin with aldehydes led to changes in the light emission of the bioluminescent protein, aequorin. The light emission was spectrofluorometrically determined with a modified aequorin protein (apoaequorin) bearing various double-cysteine mutant derivatives of green florescent protein. The chemiluminescence spectra of the adducts of hemoglobin with aldehydes obtained by examining aequorin protein containing mutations of cysteine residues at position 535 (C535S) and 629 (C629S) exhibited an increase of light emission when compared

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