The Cryptic Nature of Fe-S Clusters: A Case Study of the Hepatitis B HBx Oncoprotein
Abstract
:1. Introduction
2. Methods for Fingerprinting Fe-S Clusters
2.1. UV/VIS Spectroscopy
2.1.1. [2Fe-2S] Clusters
2.1.2. [3Fe-4S] Clusters
2.1.3. [4Fe-4S] Clusters
2.2. Electron Paramagnetic Resonance (EPR) Spectroscopy
2.2.1. [2Fe-2S] Clusters
2.2.2. [3Fe-4S] Clusters
2.2.3. [4Fe-4S] Clusters
2.3. Mössbauer Spectroscopy
2.3.1. [2Fe-2S] Clusters
System | Formal Valence | δ (mm/s) | |ΔEQav| (mm/s) |
---|---|---|---|
[2Fe-2S]2+ | |||
Rieske (CCHH) [38] | Fe3+ Fe3+ | 0.24 0.32 | 0.52 0.91 |
mitoNEET (CCCH) | Fe3+ Fe3+ | 0.26 0.30 | 0.47 0.96 |
IscR (CCCH) [35] | Fe3+ Fe3+ | 0.27 0.30 | 0.48 0.72 |
Grx3 (CC(GSH)2) [52] | Fe3+ Fe2+ | 0.29 0.29 | 0.55 0.76 |
Grx-Fra2 (CHXGSH) [52] | Fe3+ Fe2+ | 0.30 0.32 | 0.50 0.82 |
IscU (CCCD) [90] | Fe3+ Fe3+ | 0.27 0.32 | 0.66 0.94 |
Apd1/Aim32 (CCHH) [36] | Fe3+ Fe3+ | 0.24 0.35 | 0.54 1.06 |
RsrR (CCHE) [60,61] | Fe3+ Fe3+ | 0.28 0.29 | 0.54 0.76 |
Biotin synthase (CCCR) [57,58] | Fe3+ Fe3+ | 0.29 0.29 | 0.51 0.51 |
[2Fe-2S]1+ | |||
Rieske (CCHH) [38] | Fe3+ Fe2+ | 0.31 0.74 | 0.63 3.05 |
mitoNEET (CCCH) [34] | Fe3+ Fe2+ | 0.32 0.68 | 1.07 3.15 |
IscR CCCH [35] | Fe3+ Fe2+ | 0.33 0.70 | 1.09 3.40 |
Apd1/Aim32 (CCHH) [36] | Fe3+ Fe2+ | 0.32 0.75 | 0.81 3.16 |
2.3.2. [3Fe-4S] Clusters
2.3.3. [4Fe-4S] Clusters
2.4. Supplementary or Alternative Approaches
2.4.1. Chemoproteomics
2.4.2. Pulse EPR
2.4.3. NMR Spectroscopy
3. Identification of a Fe-S Cluster in the Hepatitis Virus HBx Oncoprotein
3.1. The Hepatitis Virus HBx
3.2. Spectroscopic Identification of the Cofactor
3.3. Whole-Cell Mössbauer Studies to Establish the Physiological Fe-S Cluster Form in HBx
3.4. Redox Transformations of the HBx Fe-S Cluster
3.5. HBx Preferentially Binds a Fe-S Cluster and Not Zn
4. Conclusions
Author Contributions
Funding
Data Availability Statement
Acknowledgments
Conflicts of Interest
References
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Coordination | Protein | Stot | (g1, g2, g3) a | gav | Temperature (K) a,b |
---|---|---|---|---|---|
[2Fe-2S]1+ | |||||
CCCC | Mitochondrial FXD1 [48] | 1/2 | 2.03, 1.94, 1.94 | 1.97 | 4–100 |
Vegetative Fd [49] | 1/2 | 2.05, 1.95, 1.88 | 1.96 | 4–100 | |
HydC thioredoxin-like [50] | 1/2 | 2.01, 1.95, 1.92 | 1.96 | 40 | |
CC(GSH)2 | Glrx3 [51] | 1/2 | 2.01, 1.97, 1.92 | 1.97 | 26 |
Grx3 [52] | 1/2 | 2.03, 1.94, 1.94 | 1.97 | 26 | |
Grx4 [53] | 1/2 | 2.03, 1.94, 1.94 | 1.97 | 20 | |
CCCH | mitoNEET [54,55] | 1/2 | 2.01, 1.94, 1.90 | 1.95 | 5–60 |
Miner1 [55] | 1/2 | 2.01, 1.94, 1.90 | 1.95 | 20 | |
Miner2 [55] Miner2 [55] | 1/2 1/2 | 2.00, 1.92, 1.90 2.01, 1.94, 1.89 | 1.94 1.95 | 20 20 | |
IscR [9,35] | 1/2 | 1.99, 1.93, 1.88 | 1.93 | 20 | |
CC(GSH)H | Glrx3−BolA2 [51] | 1/2 | 2.01, 1.91, 1.88 | 1.93 | 26 |
Grx3-Fra2 C [52,56] | 1/2 | 2.01, 1.92, 1.87 | 1.93 | 4–70 | |
Glrx4-IbaG C [53] | 1/2 | 2.01, 1.92, 1.87 | 1.93 | 20 | |
CCCR | Biotin synthase [57,58] | 1/2 | 2.03, 1.95, 1.90 | 1.96 | 6–80 |
CCHH | Rieske [38] | 1/2 | 2.02, 1.90, 1.80 | 1.91 | 4–100 |
Apd1 [36] | 1/2 | 2.01, 1.91, 1.86 | 1.93 | 10 | |
C(GSH)HH | GrxS14-BolA1 [59] | 1/2 | 2.02, 1.96, 1.65 | 1.88 | 10 |
CCHE | RsrR [60,61] | 1/2 | 2.00, 1.92, 1.87 | 1.93 | 10 |
[3Fe-4S]1+ | |||||
CCC cube | [NiFe] hydrogenase [62] | 1/2 | 2.02, 2.00, 1.97 | 2.00 | 2–12 |
CCC linear | GciS [25] | 5/2 | 9.10, 4.30, 4.15 | 5.85 | 4–40 |
[4Fe-4S]3+ | |||||
CCCC | HiPIP [41,63,64] | 1/2 | 2.12, 2.03, 2.03 | 2.06 | 4–20 |
[4Fe-4S]1+ | |||||
CCCC | Super-reduced HiPIP [64] | 1/2 | 2.04, 1.92, 1.92 | 1.96 | 4–40 |
NuoG [65] | 1/2 | 2.06, 1.94, 1.89 | 1.96 | 4–60 | |
DMSO reductase [66] | 1/2 | 2.03, 1.94, 1.94 | 1.97 | 4–30 | |
NfuA [67] | 1/2 | 2.04, 1.95, 1.90 | 1.96 | 5–35 | |
CCCH | [FeFe]-hydrogenase I [68] [FeFe]-hydrogenase I [68] [FeFe]-hydrogenase I [68] | 1/2 | 2.07, 1.93, 1.87 | 1.96 | 4–20 |
3/2 | 5.60, 1.71, 1.31 | 2.87 | 4–30 | ||
7/2 | 5.21, 5.13, 4.91 | 5.08 | 4–80 | ||
HydF [69] | 1/2 | 2.04, 1.90, 1.85 | 1.93 | 10 | |
CCCD | FNR [70,71] | 1/2 | 2.05, 1.94, 1.89 | 1.96 | 15 |
NsrR [72] | 1/2 | 2.04, 1.93, 1.93 | 1.97 | 10 | |
Fd [73] | 1/2 | 2.10, 1.87, 1.80 | 1.92 | 4–15 | |
CCCS | LipA Aux [74] | 1/2 | 2.05, 1.91, 1.91 | 1.96 | 13 |
CCC(H2O) | Aconitase [39] | 1/2 | 2.06, 1.93, 1.86 | 1.95 | 13 |
CCC(citrate) | Aconitase + citrate [39] | 1/2 | 2.04, 1.85, 1.78 | 1.89 | 13 |
CCC(H2O)-RS | PFL-AE [40] | 1/2 | 2.02, 1.94, 1.88 | 1.95 | 12 |
RimO [75] | 1/2 | 2.04, 1.93, 1.93 | 1.97 | 14 | |
CCC(SAM)-RS | PFL-AE + SAM [40] | 1/2 | 2.01, 1.89, 1.88 | 1.93 | 4–40 |
RimO + SAM [75] | 1/2 | 2.04, 1.93, 1.93 | 1.97 | 14 |
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Quist, T.; Chen, J.; MacNeil, A.; Pandelia, M.-E. The Cryptic Nature of Fe-S Clusters: A Case Study of the Hepatitis B HBx Oncoprotein. Inorganics 2023, 11, 475. https://doi.org/10.3390/inorganics11120475
Quist T, Chen J, MacNeil A, Pandelia M-E. The Cryptic Nature of Fe-S Clusters: A Case Study of the Hepatitis B HBx Oncoprotein. Inorganics. 2023; 11(12):475. https://doi.org/10.3390/inorganics11120475
Chicago/Turabian StyleQuist, Trent, Jiahua Chen, Alex MacNeil, and Maria-Eirini Pandelia. 2023. "The Cryptic Nature of Fe-S Clusters: A Case Study of the Hepatitis B HBx Oncoprotein" Inorganics 11, no. 12: 475. https://doi.org/10.3390/inorganics11120475