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The protein resembles the c\u2010subunit of bacterial twin\u2010arginine\u2010motif\u2010dependent protein translocases (TatC). Using native prefractionation of mitochondrial protein complexes from Arabidopsis and trapped\u2010ion mobility spectrometry (TIMS) time\u2010of\u2010flight mass spectrometry, we report the identification of three peptides of the\n                    <jats:italic>orfx<\/jats:italic>\n                    protein. Our experimental approach was used to trace the native forms of the protein and show that it is present in protein complexes in the size range of 450\u2013530\u2009kDa, which also contain TatB. We suggest that mitochondrial TatBC complexes in plants may bind to late assembly intermediates of respiratory chain complex III.\n                  <\/jats:p>","DOI":"10.1002\/1873-3468.70417","type":"journal-article","created":{"date-parts":[[2026,7,21]],"date-time":"2026-07-21T06:55:03Z","timestamp":1784616903000},"page":"2117-2128","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Identification of the plant mitochondrial\n                    <scp>\n                      <i>OrfX<\/i>\n                    <\/scp>\n                    protein: A\u00a0mass spectrometry approach"],"prefix":"10.1002","volume":"600","author":[{"ORCID":"https:\/\/orcid.org\/0009-0006-7357-9350","authenticated-orcid":false,"given":"Matthias","family":"D\u00f6ring","sequence":"first","affiliation":[{"name":"Institute of Plant Genetics Leibniz Universit\u00e4t Hannover  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