{"doi":"10.1101/2024.04.26.590571","title":"Cryo-EM captures the coordination of long-range allostery and asymmetric electron transfer by a bi-copper cluster in the nitrogenase-like DPOR complex","abstract":"Abstract Enzymes that catalyze long-range electron transfer reactions are often structurally evolved to possess two symmetrical halves. The functional advantages and mechanistic principles for such architecture remain a mystery. Using Cryo-EM we capture snapshots of the nitrogenase-like Dark-operative Protochlorophyllide Oxidoreductase (DPOR) enzyme during substrate recognition and turnover. The structures reveal that asymmetry is enforced upon substrate binding and leads to an allosteric inhibition of protein-protein interactions and electron transfer in one half. Residues that form a conduit for electron transfer are aligned in one half while misaligned in the other. An ATP-turnover coupled switch is triggered once electron transfer is accomplished in one half and relayed through a bi-copper cluster at the oligomeric interface, leading to activation of enzymatic events in the other. The findings provide a mechanistic blueprint for regulation of asymmetric long-range electron transfer. One-Sentence Summary A bi-copper cluster coordinates electron transfer for substrate reduction in the nitrogenase-like DPOR enzyme and the structures reveal how allostery and asymmetry are enacted over 100Å and utilized for sequential electron transfer.","journal":"bioRxiv (Cold Spring Harbor Laboratory)","year":2024,"id":497137,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":0,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.9481,"is_data_producer":false,"deposit_databanks":null,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2024-01-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":477330,"name":"Jaigeeth Deveryshetty","orcid":"0000-0003-1979-4085","position":1,"is_corresponding":false},{"id":1343752,"name":"Natalie Walsh","orcid":"0009-0004-5038-2163","position":2,"is_corresponding":false},{"id":437931,"name":"Monika Tokmina‐Lukaszewska","orcid":"0000-0003-3298-8298","position":3,"is_corresponding":false},{"id":316553,"name":"Brian Bothner","orcid":"0000-0003-1295-9609","position":4,"is_corresponding":false},{"id":452633,"name":"Brian Bennett","orcid":"0000-0003-2688-1478","position":5,"is_corresponding":false},{"id":452634,"name":"Edwin Antony","orcid":"0000-0002-1888-054X","position":6,"is_corresponding":false},{"id":1343751,"name":"R. P. KASHYAP","orcid":"0000-0002-9141-1168","position":0,"is_corresponding":true}],"reference_count":26,"raw_metadata":null,"created_at":"2026-07-19T02:09:30.779495Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}