Title : Redox heme-proteins mediated fluorescence of CdSe/ZnS quantum dots.

Pub. Date : 2014 Apr 5

PMID : 24705372






3 Functional Relationships(s)
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1 The redox properties of cytochrome c (Cyt c), hemoglobin (Hb) and myoglobin (Mb) were studied based on electrostatic interactions between Thioglycolic acid (TGA) capped CdSe/ZnS quantum dots (QDs) and proteins. 2-mercaptoacetate cytochrome c, somatic Homo sapiens
2 The redox properties of cytochrome c (Cyt c), hemoglobin (Hb) and myoglobin (Mb) were studied based on electrostatic interactions between Thioglycolic acid (TGA) capped CdSe/ZnS quantum dots (QDs) and proteins. 2-mercaptoacetate cytochrome c, somatic Homo sapiens
3 The redox properties of cytochrome c (Cyt c), hemoglobin (Hb) and myoglobin (Mb) were studied based on electrostatic interactions between Thioglycolic acid (TGA) capped CdSe/ZnS quantum dots (QDs) and proteins. 2-mercaptoacetate cytochrome c, somatic Homo sapiens