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Immunological relationship among hydrogenases
K L Kovacs1, L C Seefeldt, G Tigyi
1Department of Biochemistry, University of Georgia, Athens 30602.
Journal of Bacteriology
|January 1, 1989
Summary
Immunological studies reveal distinct subunits in nickel-iron (Ni-Fe) hydrogenases, with conserved regions in large subunits but less conservation in small subunits across species. Iron-only (Fe-only) hydrogenases show varied cross-reactivity, indicating unique evolutionary paths.
Area of Science:
- Biochemistry
- Immunology
- Microbial Physiology
Background:
- Hydrogenases are crucial enzymes catalyzing hydrogen oxidation or evolution.
- Understanding hydrogenase structure-function relationships is vital for bioenergy applications.
- Immunological comparisons can reveal evolutionary relationships and conserved domains.
Purpose of the Study:
- To investigate immunological cross-reactivity among diverse hydrogenase antigens and antibodies.
- To explore the immunological distinctness of hydrogenase subunits.
- To assess interspecies conservation and relationships among different hydrogenase types.
Main Methods:
- Utilized 11 different hydrogenase antigens and 9 different hydrogenase antibodies.
- Examined antibodies and antigens from both subunits of Ni-Fe hydrogenases from Bradyrhizobium japonicum and Thiocapsa roseopersicina.
- Tested cross-reactivity between antibodies to Clostridium pasteurianum hydrogenases and other Fe-only and Ni-Fe hydrogenases.
Main Results:
- Demonstrated strong immunological relationships among Ni-Fe dimeric hydrogenases.
- Showed that the 60-kDa and 30-kDa subunits of Ni-Fe hydrogenases are immunologically distinct.
- Identified conserved regions in large subunits across species, while small subunits showed less conservation.
- Observed cross-reactivity between antibodies to Clostridium pasteurianum bidirectional hydrogenase and Desulfovibrio vulgaris bidirectional hydrogenase.
- Found surprising cross-reactivity of clostridial uptake hydrogenase antibodies with Ni-Fe hydrogenases, but not Fe-only hydrogenases.
- Highlighted significant immunological differences between the two hydrogenases from C. pasteurianum.
Conclusions:
- Ni-Fe hydrogenase subunits possess distinct immunological properties, suggesting specific functional roles.
- Conserved epitopes in large subunits facilitate interspecies cross-reactivity, indicating functional importance.
- Fe-only and Ni-Fe hydrogenases exhibit diverse immunological profiles, reflecting distinct evolutionary trajectories.
- The immunological data provide insights into hydrogenase structure, function, and evolution.