Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870811 | FEBS Letters | 2013 | 7 Pages |
Abstract
Sulfonucleotide reductases catalyse the first reductive step of sulfate assimilation. Their substrate specificities generally correlate with the requirement for a [Fe4S4] cluster, where adenosine 5â²-phosphosulfate (APS) reductases possess a cluster and 3â²-phosphoadenosine 5â²-phosphosulfate reductases do not. The exception is the APR-B isoform of APS reductase from the moss Physcomitrella patens, which lacks a cluster. The crystal structure of APR-B, the first for a plant sulfonucleotide reductase, is consistent with a preference for APS. Structural conservation with bacterial APS reductase rules out a structural role for the cluster, but supports the contention that it enhances the activity of conventional APS reductases.
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Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Clare E.M. Stevenson, Richard K. Hughes, Michael T. McManus, David M. Lawson, Stanislav Kopriva,