Sequence-specific Assignment of the 1H and 15N Nuclear Magnetic Resonance
Spectra of the Reduced Recombinant High-potential Iron-sulfur Protein I from
Ectothiorhodospira halophila

Bertini, I., Felli, I. C., Kastrau, D. H.W., Luchinat,
C., Piccioli, M., and Viezzoli, M. S., "Sequence-specific
assignment of the 1H and 15N nuclear magnetic resonance
spectra of the reduced recombinant high potential iron-sulfur
protein I from Ectothiorhodospira halophila," European Journal
of Biochemistry 225, 703-714 (1994).

Sequence-specific assignment of the 1H and 15N nuclear magnetic resonance spectra of the reduced recombinant high-potential iron-sulfur protein I from Ectothiorhodospira halophila.

HiPIP (high-potential iron-sulfur protein) I

The Three Dimensional Structure Of The Paramagnetic Protein Hipip I From E.Halophila Through Nuclear Magnetic Resonance

The Molecular Structure Of The High Potential Iron-Sulfur Protein Isolated From Ectothiorhodospira Halophila Determined At 2.5-

RecName: Full=High-potential iron-sulfur protein isozyme I; AltName: Full=HiPIP 1; AltName: Full=High-redox-potential ferredoxi

Wild-type does not contain Ala1 and Ser2