Journal
INORGANICA CHIMICA ACTA
Volume 514, Issue -, Pages -Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.ica.2020.119984
Keywords
Paramagnetic NMR; Metalloproteins; Biological inorganic chemistry; Metal ion in biological systems; HIPIP; Iron-sulfur proteins
Categories
Funding
- European EC Horizon 2020 TIMB3 [810856, PID 4509]
- COST Action [CA15133]
- COST (European Cooperation in Science and Technology)
- Fondazione Ente Cassa di Risparmio di Firenze [CRF 2016 0985]
- national funds through FCT-Fundacao para a Ciencia e a Tecnologia, I.P. [UIDB/04612/2020, UIDP/04612/2020]
- Fundacao para a Ciencia e a Tecnologia (FCT) Portugal [PD/BD/135187/2017]
- Fundação para a Ciência e a Tecnologia [UIDB/04612/2020, PD/BD/135187/2017, UIDP/04612/2020] Funding Source: FCT
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Assigning H-1, C-13 and N-15 protein signals becomes challenging in the presence of a paramagnetic center. Tailored experiments and optimizations can help overcome the difficulties and obtain complete resonance assignment.
The complete assignment of H-1, C-13 and N-15 protein signals, which is a straightforward task for diamagnetic proteins provided they are folded, soluble and with a molecular mass below 30,000 Da, often becomes an intractable problem in the presence of a paramagnetic center. Indeed, the hyperfine interaction quenches signal intensity; this prevents the detection of scalar and dipolar connectivities and the sequential assignment of protein regions close to the metal ion(s). However, many experiments can be optimized and novel experiments can be designed to circumvent the problem and to revive coherences invisible in standard experiments. The small HiPIP protein PioC provides an interesting case to address this issue: the prosthetic group is a [Fe4S4](2+) cluster that is bound to the 54 amino acids protein via four cysteine residues. The four cluster-bound cysteine residues adopt different binding conformations and therefore each cysteine is affected by paramagnetic relaxation to different extent. A network of tailored experiments succeeded to obtain the complete resonance assignment of cluster bound residues.
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