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</script>pmid: 15540590
Abstract The structure elucidation of the cyclic (lactonic) forms of the pyoverdins with a succinamide side chain originally produced by the closely related species Pseudomonas syringae and P. cichorii is reported. Mass spectrometry and nuclear magnetic resonance analyses as well as the determination of the configuration of the amino acids after degradation indicate that these two pyoverdins differ only by the replacement of the first in-chain serine by glycine. The pyoverdins of P. syringae and P. cichorii and the dihydropyoverdin of P. syringae can be used by both species as siderophores.
Molecular Weight, Magnetic Resonance Spectroscopy, Protein Conformation, Pseudomonas, Pseudomonas syringae, Siderophores, Amino Acid Sequence, Amino Acids, Oligopeptides
Molecular Weight, Magnetic Resonance Spectroscopy, Protein Conformation, Pseudomonas, Pseudomonas syringae, Siderophores, Amino Acid Sequence, Amino Acids, Oligopeptides
| citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 22 | |
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| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Average | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
