The energy landscapes of proteins are highly complex and can be influenced by changes in physical and chemical conditions under which the protein is studied. The redox enzyme cytochrome P450cam undergoes a multistep catalytic cycle wherein two electrons are transferred to the heme group and the enzyme visits several conformational states. Using paramagnetic NMR spectroscopy with a lanthanoid tag, we show that the enzyme bound to its redox partner, putidaredoxin, is in a closed state at ambient temperature in solution. This result contrasts with recent crystal structures of the complex, which suggest that the enzyme opens up when bound to its partner. The closed state supports a model of catalysis in which the substrate is locked in the active site pocket and the enzyme acts as an insulator for the reactive intermediates of the reaction. The ubiquitous enzymes called cytochromes P450 catalyze a broad range of chemical reactions using molecular oxygen. For example, in humans, these enzymes are involved in breakdown of foreign compounds, including drugs. The bacterial cytochrome P450cam is thought to open up to allow substrate to enter the active site, and then to close during catalysis to keep reactive intermediates inside. Surprisingly, recent crystal structures suggested that the enzyme is open during the reaction. We have studied the enzyme in solution using paramagnetic NMR spectroscopy, demonstrating that, in fact, the enzyme is closed. This finding indicates that the subtle balance between open and closed is affected by crystallization, which can lead to the wrong conclusions about the protein dynamics.