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. 1984 Jul;81(14):4246–4249. doi: 10.1073/pnas.81.14.4246

Use of riboflavin-binding protein to investigate steric and electronic relationships in flavin analogs and models.

A Wessiak, L M Schopfer, L C Yuan, T C Bruice, V Massey
PMCID: PMC345564  PMID: 6589590

Abstract

We have examined the affinity of two recently synthesized flavin analogs for the isoalloxazine binding site of riboflavin-binding protein (RBP). The results showed that pyrimidopteridines could bind to RBP (Kd 160-250 microM). This suggested that, at the FMN or FAD level, these analogs might also bind to other apoflavoproteins, thereby providing a high potential probe for flavin enzymology. In contrast, 4a,5-ring-opened isoalloxazines did not bind to RBP. However, 1,10a-ring-opened flavins bind with considerable avidity (Kd about 40 nM). Evidence is presented which indicates that the 4a,5-ring-opened species adopted a nonplanar configuration which, in turn, was responsible for the lack of affinity to RBP. Steric and electronic consequences of a 4a,5 ring opening are discussed in relation to flavin-dependent phenolic hydroxylases.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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